MolNFT v1 · #176067 · protein
Adenosine triphosphate phosphoribosyltransferase from vibrio cholerae in complex with ATP and prpp
7DAH: “Adenosine triphosphate phosphoribosyltransferase from vibrio cholerae in complex with ATP and prpp”. X-ray diffraction, 4 ligands (ATP, PRP, MG). MolNFT v1 #176067 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7DAH
- Type
- protein
- Length
- 1,735 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- C3LU29
- Ligands
- ATP, PRP, MG, PO4
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 288 | — | C3LU29 |
| B | — | protein | 292 | — | C3LU29 |
| C | — | protein | 288 | — | C3LU29 |
| D | — | protein | 287 | — | C3LU29 |
| E | — | protein | 293 | — | C3LU29 |
| F | — | protein | 287 | — | C3LU29 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains C, F
- PRP · 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose · ligand · 2 copies · chains A, C, D, F
- MG · Magnesium ion · metal · 2 copies · chains C, F
- PO4 · Phosphate ion · ion · 2 copies · chains A, D
- EDO · 1,2-ethanediol · additive · 8 copies · chains A, C, D, F, E
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, D
- GOL · Glycerol · additive · 2 copies · chains A, C, D, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7DAH · Adenosine triphosphate phosphoribosyltransferase from Vibrio cholerae in complex with ATP… · the same entry in another collection · chain A against A, 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 C3LU29
- Elsewhere: RCSB PDB 7DAH · PDBe 7DAH · UniProt C3LU29
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