MolNFT v1 · #51851 · protein
Formyl-CoA transferase mutant variant G260A
2VJN · Formyl-coenzyme a transferase: “Formyl-CoA transferase mutant variant G260A”. X-ray diffraction, 10 pockets (best druggability 0.80). MolNFT v1 #51851 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2VJN
- Type
- protein
- Length
- 854 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Formyl-coenzyme a transferase
- EC
- 2.8.3.16
- UniProt
- O06644
- Pockets
- 10 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Formyl-coenzyme a transferase (EC 2.8.3.16) | protein | 427 | 39% helix, 13% strand | O06644 |
Ligands and binding sites
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 725 | 0.80 | 0.84 | 102 | empty |
| 2 | 431 | 0.70 | 0.81 | 58 | empty |
| 3 | 126 | 0.60 | 0.85 | 40 | empty |
| 4 | 204 | 0.59 | 0.81 | 27 | empty |
| 5 | 353 | 0.58 | 0.76 | 39 | EPE |
Interfaces
1 interface between chains.
- A–B · 6163 Ų buried · 75 hydrogen bonds · protein-protein
Compared structures
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 O06644
- Elsewhere: RCSB PDB 2VJN · PDBe 2VJN · UniProt O06644
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