MolNFT v1 · #160171 · protein
Mechanism for regulation of DNA binding of bordetella bronchiseptica bpsr by 6-hydroxynicotinic acid
6PCP: “Mechanism for regulation of DNA binding of bordetella bronchiseptica bpsr by 6-hydroxynicotinic acid”. X-ray diffraction, 1 ligand (OA7). MolNFT v1 #160171 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PCP
- Type
- protein
- Length
- 834 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0T7MD48
- Ligands
- OA7
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F | — | protein | 140 | — | A0A0T7MD48 |
| B | — | protein | 135 | — | A0A0T7MD48 |
| C, E | — | protein | 140 | — | A0A0T7MD48 |
| D | — | protein | 139 | — | A0A0T7MD48 |
Ligands and binding sites
- OA7 · 6-hydroxypyridine-3-carboxylic acid · ligand · 6 copies · chains A, D, B, C, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PCP · Mechanism for regulation of DNA binding of Bordetella bronchiseptica BpsR by… · 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 A0A0T7MD48
- Elsewhere: RCSB PDB 6PCP · PDBe 6PCP · UniProt A0A0T7MD48
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