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Structure of 2,5-dihydroxypridine dioxygenase from pseudomonas putida KT2440 in complex with product N-formylmaleamic acid formed via in crystallo reaction with 2,5-dihydroxypridine
Analyse Structure of 2,5-dihydroxypridine dioxygenase from pseudomonas putida KT2440 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CNT
- Type
- protein
- Length
- 2,088 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q88FY1
- Ligands
- FE2
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 348 | — | Q88FY1 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7CNT · Structure of 2,5-dihydroxypridine Dioxygenase from Pseudomonas putida KT2440 in complex… · the same entry in another collection · chain C against C, TM-score 1.00
- Q88FY1 · AlphaFold monomer V2.0 prediction for 2,5-dihydroxypyridine 5,6-dioxygenase (Q88FY1) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q88FY1
- Elsewhere: RCSB PDB 7CNT · PDBe 7CNT · UniProt Q88FY1
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