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39  structures 1596  species 0  interactions 70727  sequences 1403  architectures

Family: zf-RING_2 (PF13639)

Summary: Ring finger domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "RING finger domain". More...

RING finger domain Edit Wikipedia article

Zinc finger, C3HC4 type (RING finger)
1chc animated.gif
Structure of the C3HC4 domain.[1] Zinc ions are black spheres, coordinated by cysteines residues (blue).
Identifiers
Symbolzf-C3HC4
PfamPF00097
InterProIPR001841
SMARTSM00184
PROSITEPDOC00449
SCOPe1chc / SUPFAM

In molecular biology, a RING (Really Interesting New Gene) finger domain is a protein structural domain of zinc finger type which contains a C3HC4 amino acid motif which binds two zinc cations (seven cysteines and one histidine arranged non-consecutively).[2][3][4][5] This protein domain contains from 40 to 60 amino acids. Many proteins containing a RING finger play a key role in the ubiquitination pathway.

Zinc fingers

Zinc finger (Znf) domains are relatively small protein motifs that bind one or more zinc atoms, and which usually contain multiple finger-like protrusions that make tandem contacts with their target molecule. They bind DNA, RNA, protein and/or lipid substrates.[6][7][8][9][10] Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing.[11] Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

Some Zn finger domains have diverged such that they still maintain their core structure, but have lost their ability to bind zinc, using other means such as salt bridges or binding to other metals to stabilise the finger-like folds.

Function

Many RING finger domains simultaneously bind ubiquitination enzymes and their substrates and hence function as ligases. Ubiquitination in turn targets the substrate protein for degradation.[12][13][14]

Structure

The RING finger domain has the consensus sequence C-X2-C-X[9-39]-C-X[1-3]-H-X[2-3]-C-X2-C-X[4-48]-C-X2-C.[2] where:

  • C is a conserved cysteine residue involved zinc coordination,
  • H is a conserved histidine involved in zinc coordination,
  • Zn is zinc atom, and
  • X is any amino acid residue.

The following is a schematic representation of the structure of the RING finger domain:[2]

                              x x x     x x x
                             x      x x      x
                            x       x x       x
                           x        x x        x
                          C        C   C        C
                         x  \    / x   x \    /  x
                         x    Zn   x   x   Zn    x
                          C /    \ H   C /    \ C
                          x         x x         x
                 x x x x x x         x         x x x x x x

Examples

Examples of human genes which encode proteins containing a RING finger domain include:

AMFR, BBAP, BFAR, BIRC2, BIRC3, BIRC7, BIRC8, BMI1, BRAP, BRCA1, CBL, CBLB, CBLC, CBLL1, CHFR, COMMD3, DTX1, DTX2, DTX3, DTX3L, DTX4, DZIP3, HCGV, HLTF, HOIL-1, IRF2BP2, LNX1, LNX2, LONRF1, LONRF2, LONRF3, MARCH1, MARCH10, MARCH2, MARCH3, MARCH4, MARCH5, MARCH6, MARCH7, MARCH8, MARCH9, MDM2, MEX3A, MEX3B, MEX3C, MEX3D, MGRN1, MIB1, MID1, MID2, MKRN1, MKRN2, MKRN3, MKRN4, MNAT1, MYLIP, NFX1, NFX2, PCGF1, PCGF2, PCGF3, PCGF4, PCGF5, PCGF6, PDZRN3, PDZRN4, PEX10, PHRF1, PJA1, PJA2, PML, PML-RAR, PXMP3, RAD18, RAG1, RAPSN, RBCK1, RBX1, RC3H1, RC3H2, RCHY1, RFP2, RFPL1, RFPL2, RFPL3, RFPL4B, RFWD2, RFWD3, RING1, RNF2, RNF4, RNF5, RNF6, RNF7, RNF8, RNF10, RNF11, RNF12, RNF13, RNF14, RNF19A, RNF20, RNF24, RNF25, RNF26, RNF32, RNF38, RNF39, RNF40, RNF41, RNF43, RNF44, RNF55, RNF71, RNF103, RNF111, RNF113A, RNF113B, RNF121, RNF122, RNF123, RNF125, RNF126, RNF128, RNF130, RNF133, RNF135, RNF138, RNF139, RNF141, RNF144A, RNF145, RNF146, RNF148, RNF149, RNF150, RNF151, RNF152, RNF157, RNF165, RNF166, RNF167, RNF168, RNF169, RNF170, RNF175, RNF180, RNF181, RNF182, RNF185, RNF207, RNF213, RNF215, RNFT1, SH3MD4, SH3RF1, SH3RF2, SYVN1, TIF1, TMEM118, TOPORS, TRAF2, TRAF3, TRAF4, TRAF5, TRAF6, TRAF7, TRAIP, TRIM2, TRIM3, TRIM4, TRIM5, TRIM6, TRIM7, TRIM8, TRIM9, TRIM10, TRIM11, TRIM13, TRIM15, TRIM17, TRIM21, TRIM22, TRIM23, TRIM24, TRIM25, TRIM26, TRIM27, TRIM28, TRIM31, TRIM32, TRIM33, TRIM34, TRIM35, TRIM36, TRIM38, TRIM39, TRIM40, TRIM41, TRIM42, TRIM43, TRIM45, TRIM46, TRIM47, TRIM48, TRIM49, TRIM50, TRIM52, TRIM54, TRIM55, TRIM56, TRIM58, TRIM59, TRIM60, TRIM61, TRIM62, TRIM63, TRIM65, TRIM67, TRIM68, TRIM69, TRIM71, TRIM72, TRIM73, TRIM74, TRIML1, TTC3, UHRF1, UHRF2, VPS11, VPS8, ZNF179, ZNF294, ZNF313, ZNF364, ZNF650, ZNFB7, ZNRF1, ZNRF2, ZNRF3, ZNRF4, and ZSWIM2.

References

  1. ^ Barlow PN, Luisi B, Milner A, Elliott M, Everett R (March 1994). "Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc-finger". J. Mol. Biol. 237 (2): 201–11. doi:10.1006/jmbi.1994.1222. PMID 8126734.
  2. ^ a b c Borden KL, Freemont PS (1996). "The RING finger domain: a recent example of a sequence-structure family". Curr. Opin. Struct. Biol. 6 (3): 395–401. doi:10.1016/S0959-440X(96)80060-1. PMID 8804826.
  3. ^ Hanson IM, Poustka A, Trowsdale J (1991). "New genes in the class II region of the human major histocompatibility complex". Genomics. 10 (2): 417–24. doi:10.1016/0888-7543(91)90327-B. PMID 1906426.
  4. ^ Freemont PS, Hanson IM, Trowsdale J (1991). "A novel cysteine-rich sequence motif". Cell. 64 (3): 483–4. doi:10.1016/0092-8674(91)90229-R. PMID 1991318.
  5. ^ Lovering R, Hanson IM, Borden KL, Martin S, O'Reilly NJ, Evan GI, Rahman D, Pappin DJ, Trowsdale J, Freemont PS (1993). "Identification and preliminary characterization of a protein motif related to the zinc finger". Proc. Natl. Acad. Sci. U.S.A. 90 (6): 2112–6. doi:10.1073/pnas.90.6.2112. PMC 46035. PMID 7681583.
  6. ^ Klug A (1999). "Zinc finger peptides for the regulation of gene expression". J. Mol. Biol. 293 (2): 215–8. doi:10.1006/jmbi.1999.3007. PMID 10529348.
  7. ^ Hall TM (2005). "Multiple modes of RNA recognition by zinc finger proteins". Curr. Opin. Struct. Biol. 15 (3): 367–73. doi:10.1016/j.sbi.2005.04.004. PMID 15963892.
  8. ^ Brown RS (2005). "Zinc finger proteins: getting a grip on RNA". Curr. Opin. Struct. Biol. 15 (1): 94–8. doi:10.1016/j.sbi.2005.01.006. PMID 15718139.
  9. ^ Gamsjaeger R, Liew CK, Loughlin FE, Crossley M, Mackay JP (2007). "Sticky fingers: zinc-fingers as protein-recognition motifs". Trends Biochem. Sci. 32 (2): 63–70. doi:10.1016/j.tibs.2006.12.007. PMID 17210253.
  10. ^ Matthews JM, Sunde M (2002). "Zinc fingers--folds for many occasions". IUBMB Life. 54 (6): 351–5. doi:10.1080/15216540216035. PMID 12665246.
  11. ^ Laity JH, Lee BM, Wright PE (2001). "Zinc finger proteins: new insights into structural and functional diversity". Curr. Opin. Struct. Biol. 11 (1): 39–46. doi:10.1016/S0959-440X(00)00167-6. PMID 11179890.
  12. ^ Lorick KL, Jensen JP, Fang S, Ong AM, Hatakeyama S, Weissman AM (1999). "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination". Proc. Natl. Acad. Sci. U.S.A. 96 (20): 11364–9. doi:10.1073/pnas.96.20.11364. PMC 18039. PMID 10500182.
  13. ^ Joazeiro CA, Weissman AM (2000). "RING finger proteins: mediators of ubiquitin ligase activity". Cell. 102 (5): 549–52. doi:10.1016/S0092-8674(00)00077-5. PMID 11007473.
  14. ^ Freemont PS (2000). "RING for destruction?". Curr. Biol. 10 (2): R84–7. doi:10.1016/S0960-9822(00)00287-6. PMID 10662664.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR001841

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001841

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [ PUBMED:10529348 , PUBMED:15963892 , PUBMED:15718139 , PUBMED:17210253 , PUBMED:12665246 ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [ PUBMED:11179890 ]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

This entry represents RING-type zinc finger domains. The RING-finger is a specialised type of Zn-finger of 40 to 60 residues that binds two atoms of zinc, and is probably involved in mediating protein-protein interactions [ PUBMED:8317827 , PUBMED:8804826 , PUBMED:8744354 ]. There are two different variants, the C3HC4-type and a C3H2C3-type, which are clearly related despite the different cysteine/histidine pattern. The latter type is sometimes referred to as 'RING-H2 finger'. The RING domain is a protein interaction domain that has been implicated in a range of diverse biological processes. E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain. E3 ubiquitin-protein ligases determine the substrate specificity for ubiquitylation and have been classified into HECT and RING-finger families. More recently, however, U-box proteins, which contain a domain (the U box) of about 70 amino acids that is conserved from yeast to humans, have been identified as a new type of E3 [ PUBMED:12944364 ]. Various RING fingers also exhibit binding to E2 ubiquitin-conjugating enzymes (Ubc's) [ PUBMED:10662664 , PUBMED:10514377 , PUBMED:10577187 ].

Several 3D-structures for RING-fingers are known [ PUBMED:8804826 , PUBMED:8744354 ]. The 3D structure of the zinc ligation system is unique to the RING domain and is referred to as the 'cross-brace' motif. The spacing of the cysteines in such a domain is C-x(2)-C-x(9 to 39)-C-x(1 to 3)-H-x(2 to 3)-C-x(2)-C-x(4 to 48)-C-x(2)-C. Metal ligand pairs one and three co-ordinate to bind one zinc ion, whilst pairs two and four bind the second.

Note that in the older literature, some RING-fingers are denoted as LIM-domains. The LIM-domain Zn-finger is a fundamentally different family, albeit with similar Cys-spacing (see INTERPRO ).

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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  Seed
(165)
Full
(70727)
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RP15
(10988)
RP35
(34500)
RP55
(58512)
RP75
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(165)
Full
(70727)
Representative proteomes UniProt
(127774)
RP15
(10988)
RP35
(34500)
RP55
(58512)
RP75
(77661)
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  Seed
(165)
Full
(70727)
Representative proteomes UniProt
(127774)
RP15
(10988)
RP35
(34500)
RP55
(58512)
RP75
(77661)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Jackhmmer:Q5A9Y7
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A
Number in seed: 165
Number in full: 70727
Average length of the domain: 45.10 aa
Average identity of full alignment: 37 %
Average coverage of the sequence by the domain: 9.75 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.3 27.3
Trusted cut-off 27.3 27.3
Noise cut-off 27.2 27.2
Model length: 44
Family (HMM) version: 8
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the zf-RING_2 domain has been found. There are 39 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A096T1P3 View 3D Structure Click here
A0A0B4K658 View 3D Structure Click here
A0A0B4KHR2 View 3D Structure Click here
A0A0G2JZP9 View 3D Structure Click here
A0A0G2K9X2 View 3D Structure Click here
A0A0N7KCF9 View 3D Structure Click here
A0A0N7KFJ0 View 3D Structure Click here
A0A0N7KM84 View 3D Structure Click here
A0A0N7KPI3 View 3D Structure Click here
A0A0N7KQY8 View 3D Structure Click here
A0A0N7KTA5 View 3D Structure Click here
A0A0P0V031 View 3D Structure Click here
A0A0P0V0F7 View 3D Structure Click here
A0A0P0V0F7 View 3D Structure Click here
A0A0P0V1P8 View 3D Structure Click here
A0A0P0V3L8 View 3D Structure Click here
A0A0P0V6U1 View 3D Structure Click here
A0A0P0VES7 View 3D Structure Click here
A0A0P0VH14 View 3D Structure Click here
A0A0P0VH66 View 3D Structure Click here
A0A0P0VH66 View 3D Structure Click here
A0A0P0VIW9 View 3D Structure Click here
A0A0P0VJT9 View 3D Structure Click here
A0A0P0VKM5 View 3D Structure Click here
A0A0P0VN55 View 3D Structure Click here
A0A0P0VNZ4 View 3D Structure Click here
A0A0P0VQ82 View 3D Structure Click here
A0A0P0VQN7 View 3D Structure Click here
A0A0P0VS22 View 3D Structure Click here
A0A0P0VY10 View 3D Structure Click here
A0A0P0VY47 View 3D Structure Click here
A0A0P0VZ59 View 3D Structure Click here
A0A0P0W0Q7 View 3D Structure Click here
A0A0P0WAF2 View 3D Structure Click here
A0A0P0WAW5 View 3D Structure Click here
A0A0P0WAZ3 View 3D Structure Click here
A0A0P0WDS1 View 3D Structure Click here
A0A0P0WMA4 View 3D Structure Click here
A0A0P0WMQ2 View 3D Structure Click here
A0A0P0WNX5 View 3D Structure Click here
A0A0P0WPZ3 View 3D Structure Click here
A0A0P0WRX5 View 3D Structure Click here
A0A0P0WTV7 View 3D Structure Click here
A0A0P0WXB7 View 3D Structure Click here
A0A0P0WXD1 View 3D Structure Click here
A0A0P0WXF9 View 3D Structure Click here
A0A0P0WXH4 View 3D Structure Click here
A0A0P0WXK7 View 3D Structure Click here
A0A0P0X0S9 View 3D Structure Click here
A0A0P0X3J2 View 3D Structure Click here
A0A0P0X5D8 View 3D Structure Click here
A0A0P0XFV8 View 3D Structure Click here
A0A0P0XMT4 View 3D Structure Click here
A0A0P0XN47 View 3D Structure Click here
A0A0P0XNI1 View 3D Structure Click here
A0A0P0XPJ3 View 3D Structure Click here
A0A0P0XWT1 View 3D Structure Click here
A0A0P0XWX4 View 3D Structure Click here
A0A0P0XXU1 View 3D Structure Click here
A0A0P0XYB8 View 3D Structure Click here
A0A0P0XYC5 View 3D Structure Click here
A0A0P0XYN2 View 3D Structure Click here
A0A0P0XYP6 View 3D Structure Click here
A0A0P0XZ11 View 3D Structure Click here
A0A0P0XZ56 View 3D Structure Click here
A0A0P0Y472 View 3D Structure Click here
A0A0P0Y642 View 3D Structure Click here
A0A0P0Y659 View 3D Structure Click here
A0A0P0Y689 View 3D Structure Click here
A0A0P0Y6W5 View 3D Structure Click here
A0A0P0Y6W6 View 3D Structure Click here
A0A0P0Y731 View 3D Structure Click here
A0A0P0YC54 View 3D Structure Click here
A0A0R0E8C5 View 3D Structure Click here
A0A0R0EGM2 View 3D Structure Click here
A0A0R0EH68 View 3D Structure Click here
A0A0R0EIM7 View 3D Structure Click here
A0A0R0EQU0 View 3D Structure Click here
A0A0R0EVC5 View 3D Structure Click here
A0A0R0F3R8 View 3D Structure Click here
A0A0R0F5Z1 View 3D Structure Click here
A0A0R0F7S2 View 3D Structure Click here
A0A0R0FDQ1 View 3D Structure Click here
A0A0R0FJE2 View 3D Structure Click here
A0A0R0FPM7 View 3D Structure Click here
A0A0R0FSW3 View 3D Structure Click here
A0A0R0FYF6 View 3D Structure Click here
A0A0R0GD96 View 3D Structure Click here
A0A0R0GFS7 View 3D Structure Click here
A0A0R0GRL8 View 3D Structure Click here
A0A0R0GVR1 View 3D Structure Click here
A0A0R0H7B6 View 3D Structure Click here
A0A0R0HBH7 View 3D Structure Click here
A0A0R0HIE5 View 3D Structure Click here
A0A0R0HN88 View 3D Structure Click here
A0A0R0HSR7 View 3D Structure Click here
A0A0R0HTV4 View 3D Structure Click here
A0A0R0HVR4 View 3D Structure Click here
A0A0R0I0U2 View 3D Structure Click here
A0A0R0I7U2 View 3D Structure Click here
A0A0R0IEC7 View 3D Structure Click here
A0A0R0IF00 View 3D Structure Click here
A0A0R0IK02 View 3D Structure Click here
A0A0R0IQQ0 View 3D Structure Click here
A0A0R0IWV6 View 3D Structure Click here
A0A0R0J6F0 View 3D Structure Click here
A0A0R0JKU0 View 3D Structure Click here
A0A0R0JL04 View 3D Structure Click here
A0A0R0JLM9 View 3D Structure Click here
A0A0R0JM57 View 3D Structure Click here
A0A0R0JPQ3 View 3D Structure Click here
A0A0R0JX50 View 3D Structure Click here
A0A0R0KLB5 View 3D Structure Click here
A0A0R0KRF6 View 3D Structure Click here
A0A0R0L2G1 View 3D Structure Click here
A0A0R0L6H0 View 3D Structure Click here
A0A0R0L8N3 View 3D Structure Click here
A0A0R0LCQ0 View 3D Structure Click here
A0A0R0LF13 View 3D Structure Click here
A0A0R0LHT2 View 3D Structure Click here
A0A0R4IBU7 View 3D Structure Click here
A0A0R4IGH0 View 3D Structure Click here
A0A0R4IP89 View 3D Structure Click here
A0A0R4IPD9 View 3D Structure Click here
A0A0R4ISD3 View 3D Structure Click here
A0A0R4J308 View 3D Structure Click here
A0A0R4J3Y8 View 3D Structure Click here
A0A0R4J4G6 View 3D Structure Click here
A0A0R4J678 View 3D Structure Click here
A0A1D5NS78 View 3D Structure Click here
A0A1D5NSF2 View 3D Structure Click here
A0A1D5NT10 View 3D Structure Click here
A0A1D6E1I9 View 3D Structure Click here
A0A1D6E1Q4 View 3D Structure Click here
A0A1D6E1X9 View 3D Structure Click here
A0A1D6E1Y2 View 3D Structure Click here
A0A1D6E268 View 3D Structure Click here
A0A1D6E2F2 View 3D Structure Click here
A0A1D6E340 View 3D Structure Click here
A0A1D6E9I1 View 3D Structure Click here
A0A1D6EHE3 View 3D Structure Click here
A0A1D6EI24 View 3D Structure Click here
A0A1D6EIE2 View 3D Structure Click here
A0A1D6EMA0 View 3D Structure Click here
A0A1D6EP36 View 3D Structure Click here
A0A1D6EPG6 View 3D Structure Click here
A0A1D6ERW1 View 3D Structure Click here
A0A1D6ETY6 View 3D Structure Click here
A0A1D6EVL6 View 3D Structure Click here
A0A1D6EVN7 View 3D Structure Click here
A0A1D6EX09 View 3D Structure Click here
A0A1D6F1R4 View 3D Structure Click here
A0A1D6F2B9 View 3D Structure Click here
A0A1D6F4C7 View 3D Structure Click here
A0A1D6F4Q4 View 3D Structure Click here
A0A1D6F9Y7 View 3D Structure Click here
A0A1D6FGZ4 View 3D Structure Click here
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