3VJC: Human squalene synthase
Crystal structure of the human squalene synthase in complex with zaragozic acid A. Determined by X-ray diffraction at 1.89 Å resolution. Released 11 Apr 2012.
- Method
- X-ray diffraction
- Resolution
- 1.89 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 17,855
- Mol. weight
- 241.46 kDa
- Ligands
- MG, PO4, ZGA
- Released
- 11 Apr 2012
Explore 3VJC in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3VJC contains 141 α-helices and 0 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 23 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 38-50 | 13 | |
| α-helix | 55-59 | 5 | |
| α-helix | 64-84 | 21 | |
| α-helix | 90-103 | 14 | |
| α-helix | 120-123 | 4 | |
| α-helix | 125-134 | 10 | |
| α-helix | 137-156 | 20 | |
| α-helix | 165-172 | 8 | |
| α-helix | 173-177 | 5 | |
| α-helix | 178-190 | 13 | |
| α-helix | 195-199 | 5 | |
| α-helix | 201-218 | 18 | |
| α-helix | 220-225 | 6 | |
| α-helix | 233-236 | 4 | |
| α-helix | 243-247 | 5 | |
| α-helix | 249-251 | 3 | |
| α-helix | 252-267 | 16 | |
| α-helix | 270-279 | 10 | |
| α-helix | 283-303 | 21 | |
| α-helix | 307-310 | 4 | |
| α-helix | 323-325 | 3 | |
| α-helix | 331-348 | 18 | |
| α-helix | 356-368 | 13 | |
Chain B: 24 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 38-50 | 13 | |
| α-helix | 55-59 | 5 | |
| α-helix | 64-84 | 21 | |
| α-helix | 90-103 | 14 | |
| α-helix | 120-123 | 4 | |
| α-helix | 125-133 | 9 | |
| α-helix | 137-156 | 20 | |
| α-helix | 165-172 | 8 | |
| α-helix | 173-177 | 5 | |
| α-helix | 178-190 | 13 | |
| α-helix | 195-199 | 5 | |
| α-helix | 201-218 | 18 | |
| α-helix | 220-225 | 6 | |
| α-helix | 233-236 | 4 | |
| α-helix | 243-247 | 5 | |
| α-helix | 249-251 | 3 | |
| α-helix | 252-267 | 16 | |
| α-helix | 270-278 | 9 | |
| α-helix | 283-303 | 21 | |
| α-helix | 307-310 | 4 | |
| α-helix | 317-320 | 4 | |
| α-helix | 321-325 | 5 | |
| α-helix | 331-346 | 16 | |
| α-helix | 356-368 | 13 | |
Chain C: 23 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 38-50 | 13 | |
| α-helix | 55-59 | 5 | |
| α-helix | 63-84 | 22 | |
| α-helix | 90-103 | 14 | |
| α-helix | 120-123 | 4 | |
| α-helix | 125-134 | 10 | |
| α-helix | 137-156 | 20 | |
| α-helix | 165-172 | 8 | |
| α-helix | 173-177 | 5 | |
| α-helix | 178-189 | 12 | |
| α-helix | 195-199 | 5 | |
| α-helix | 201-218 | 18 | |
| α-helix | 220-225 | 6 | |
| α-helix | 233-236 | 4 | |
| α-helix | 243-247 | 5 | |
| α-helix | 249-251 | 3 | |
| α-helix | 252-267 | 16 | |
| α-helix | 270-278 | 9 | |
| α-helix | 283-303 | 21 | |
| α-helix | 307-310 | 4 | |
| α-helix | 321-324 | 4 | |
| α-helix | 331-348 | 18 | |
| α-helix | 356-367 | 12 | |
Chain D: 23 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 38-50 | 13 | |
| α-helix | 55-59 | 5 | |
| α-helix | 64-84 | 21 | |
| α-helix | 90-103 | 14 | |
| α-helix | 120-123 | 4 | |
| α-helix | 125-133 | 9 | |
| α-helix | 137-156 | 20 | |
| α-helix | 165-172 | 8 | |
| α-helix | 173-177 | 5 | |
| α-helix | 178-190 | 13 | |
| α-helix | 195-199 | 5 | |
| α-helix | 201-218 | 18 | |
| α-helix | 220-225 | 6 | |
| α-helix | 233-236 | 4 | |
| α-helix | 243-247 | 5 | |
| α-helix | 249-251 | 3 | |
| α-helix | 252-267 | 16 | |
| α-helix | 270-278 | 9 | |
| α-helix | 283-303 | 21 | |
| α-helix | 307-310 | 4 | |
| α-helix | 321-324 | 4 | |
| α-helix | 331-348 | 18 | |
| α-helix | 356-368 | 13 | |
Chain E: 23 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 38-50 | 13 | |
| α-helix | 55-59 | 5 | |
| α-helix | 64-84 | 21 | |
| α-helix | 90-103 | 14 | |
| α-helix | 120-123 | 4 | |
| α-helix | 125-133 | 9 | |
| α-helix | 137-156 | 20 | |
| α-helix | 165-172 | 8 | |
| α-helix | 173-177 | 5 | |
| α-helix | 178-189 | 12 | |
| α-helix | 195-199 | 5 | |
| α-helix | 201-218 | 18 | |
| α-helix | 220-225 | 6 | |
| α-helix | 233-236 | 4 | |
| α-helix | 243-247 | 5 | |
| α-helix | 249-251 | 3 | |
| α-helix | 252-267 | 16 | |
| α-helix | 270-278 | 9 | |
| α-helix | 283-303 | 21 | |
| α-helix | 307-310 | 4 | |
| α-helix | 323-325 | 3 | |
| α-helix | 331-347 | 17 | |
| α-helix | 356-366 | 11 | |
Chain F: 25 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 39-50 | 12 | |
| α-helix | 55-59 | 5 | |
| α-helix | 65-84 | 20 | |
| α-helix | 90-98 | 9 | |
| α-helix | 100-103 | 4 | |
| α-helix | 120-123 | 4 | |
| α-helix | 125-133 | 9 | |
| α-helix | 137-158 | 22 | |
| α-helix | 165-172 | 8 | |
| α-helix | 173-177 | 5 | |
| α-helix | 178-190 | 13 | |
| α-helix | 195-199 | 5 | |
| α-helix | 201-218 | 18 | |
| α-helix | 220-225 | 6 | |
| α-helix | 233-236 | 4 | |
| α-helix | 243-247 | 5 | |
| α-helix | 249-251 | 3 | |
| α-helix | 252-267 | 16 | |
| α-helix | 270-279 | 10 | |
| α-helix | 283-303 | 21 | |
| α-helix | 307-309 | 3 | |
| α-helix | 316-320 | 5 | |
| α-helix | 321-324 | 4 | |
| α-helix | 331-346 | 16 | |
| α-helix | 356-367 | 12 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Squalene synthase | A, B, C, D, E, F | protein | 343 | Homo sapiens | P37268 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>3VJC_1 Squalene synthase (chains A, B, C, D, E, F)
GSHMDQDSLSSSLKTCYKYLNQTSRSFAAVIQALDGEMRNAVCIFYLVLRALDTLEDDMT
ISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQVLEDFPTISLEFRNLAEKYQTVIADIC
RRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVGIGLSRLFSASEFEDPLVGEDTERANSM
GLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYVKKLGDFAKPENIDLAVQCLNELITNAL
HHIPDVITYLSRLRNQSVFNFCAIPQVMAIATLAACYNNQQVFKGAVKIRKGQAVTLMMD
ATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTRQIISTIRTQN
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MG | Magnesium ion | Mg | 2 |
| PO4 | Phosphate ion | O4 P | 6 |
| ZGA | Zaragozic acid A | C35 H46 O14 | 6 |
Primary citation
Binding modes of zaragozic acid A to human squalene synthase and staphylococcal dehydrosqualene synthase. Liu, C.I., Jeng, W.Y., Chang, W.J. et al. J Biol Chem (2012) 287:18750-18757. DOI 10.1074/jbc.M112.351254 · PubMed
Other PDB entries of the same protein (UniProt P37268 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6PYW 1.38 Å, Crystal Structure of HLA-B*2705-W60A in complex with LRN, a self-peptide
- 6PYJ 1.44 Å, Crystal Structure of HLA-B*2705 in complex with LRN, a self-peptide
- 6PYV 1.45 Å, Crystal Structure of HLA-B*2703-P47G in complex with LRN, a self-peptide
- 3VJ8 1.52 Å, Crystal structure of the human squalene synthase
- 3VJ9 1.52 Å, Crystal structure of the human squalene synthase
- 6PZ5 1.53 Å, Crystal Structure of HLA-B*2703 in complex with LRN, a self-peptide
- 3WEG 1.75 Å, Crystal structure of the human squalene synthase in complex with farnesyl…
- 3VJA 1.76 Å, Crystal structure of the human squalene synthase
- 3WEI 1.79 Å, Crystal structure of the human squalene synthase Y73A mutant in complex with presqualene…
- 3V66 1.8 Å, HUMAN SQUALENE SYNTHASE IN COMPLEX WITH 2-(1-{2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)…
- 3WEK 1.85 Å, Crystal structure of the human squalene synthase F288L mutant in complex with…
- 3WEH 1.87 Å, Crystal structure of the human squalene synthase in complex with presqualene pyrophosphate
Browse structure collections
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