MolNFT v1 · #183433 · protein
Vibrio cholerae PARA2-ADP
7NPE: “Vibrio cholerae PARA2-ADP”. X-ray diffraction, 2 ligands (ADP, MG). MolNFT v1 #183433 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7NPE
- Type
- protein
- Length
- 1,601 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A085S0Z4
- Ligands
- ADP, MG
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 397 | — | A0A085S0Z4 |
| B | — | protein | 402 | — | A0A085S0Z4 |
| C | — | protein | 400 | — | A0A085S0Z4 |
| D | — | protein | 402 | — | A0A085S0Z4 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
- GOL · Glycerol · additive · 2 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NPE · Vibrio cholerae ParA2-ADP · the same entry in another collection · chain B against B, 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 A0A085S0Z4
- Elsewhere: RCSB PDB 7NPE · PDBe 7NPE · UniProt A0A085S0Z4
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