MolNFT v1 · #137741 · protein
Crystal structure of catechol 1,2-dioxygenase from burkholderia ambifaria
5VXT: “Crystal structure of catechol 1,2-dioxygenase from burkholderia ambifaria”. X-ray diffraction, 4 ligands (PTY, CAQ, FE). MolNFT v1 #137741 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5VXT
- Type
- protein
- Length
- 623 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B1Z4S0
- Ligands
- PTY, CAQ, FE, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 311 | — | B1Z4S0 |
| B | — | protein | 312 | — | B1Z4S0 |
Ligands and binding sites
- PTY · Phosphatidylethanolamine · ligand · 2 copies · chains A, B
- CAQ · Catechol · ligand · 2 copies · chains A, B
- FE · Fe (III) ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5VXT · Crystal structure of catechol 1,2-dioxygenase from Burkholderia ambifaria · 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 B1Z4S0
- Elsewhere: RCSB PDB 5VXT · PDBe 5VXT · UniProt B1Z4S0
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