MolNFT v1 · #74695 · protein
Phosphoribosylformylglycinamidine cyclo-ligase from vibrio cholerae
3P4E: “Phosphoribosylformylglycinamidine cyclo-ligase from vibrio cholerae”. X-ray diffraction, 1 ligand (AMP), 2 pockets (best druggability 0.41). MolNFT v1 #74695 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3P4E
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosylformylglycinamidine cyclo-ligase
- EC
- 6.3.3.1
- UniProt
- Q9KPY6
- Ligands
- AMP
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) | protein | 323 | 38% helix, 26% strand | Q9KPY6 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
- GOL · Glycerol · additive · chains A
- CIT · Citric acid · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.41 | 0.77 | 23 | AMP |
| 2 | 50 | 0.30 | 0.76 | 12 | empty |
Compared structures
- 3P4E · Phosphoribosylformylglycinamidine cyclo-ligase from Vibrio cholerae · the same entry in another collection · chain A against A, TM-score 1.00
- Q9KPY6 · AlphaFold monomer V2.0 prediction for phosphoribosylformylglycinamidine cyclo-ligase… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9KPY6
- Elsewhere: RCSB PDB 3P4E · PDBe 3P4E · UniProt Q9KPY6
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