MolNFT v1 · #106523 · protein
Crystal structure of phosphoglycerate oxidoreductase from vibrio cholerae O395
4S1V · D-3-phosphoglycerate dehydrogenase-related protein: “Crystal structure of phosphoglycerate oxidoreductase from vibrio cholerae O395”. X-ray diffraction, 12 pockets (best druggability 0.75). MolNFT v1 #106523 on GenesisL1: 3D…
- PDB
- 4S1V
- Type
- protein
- Length
- 1,257 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-3-phosphoglycerate dehydrogenase-related protein
- EC
- 1.1.1.95
- UniProt
- A5F016
- Pockets
- 12 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | D-3-phosphoglycerate dehydrogenase-related protein (EC 1.1.1.95) | protein | 314 | 39% helix, 14% strand | A5F016 |
| A | D-3-phosphoglycerate dehydrogenase-related protein (EC 1.1.1.95) | protein | 313 | 38% helix, 16% strand | A5F016 |
| B, C | D-3-phosphoglycerate dehydrogenase-related protein (EC 1.1.1.95) | protein | 315 | 38% helix, 15% strand | A5F016 |
Pockets
12 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 610 | 0.75 | 0.82 | 82 | empty |
| 2 | 568 | 0.75 | 0.82 | 78 | empty |
| 3 | 376 | 0.74 | 0.85 | 37 | empty |
| 4 | 639 | 0.74 | 0.81 | 68 | empty |
| 5 | 538 | 0.72 | 0.81 | 47 | empty |
Interfaces
4 interfaces between chains.
- D–C · 2765 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 2751 Ų buried · 40 hydrogen bonds · protein-protein
- D–B · 517 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 466 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4S1V · Crystal structure of phosphoglycerate oxidoreductase from Vibrio Cholerae o395 · the same entry in another collection · chain D against D, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A5F016
- Elsewhere: RCSB PDB 4S1V · PDBe 4S1V · UniProt A5F016
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