Research workbench
Crystal structure of the reductase (C1) component of P- hydroxyphenylacetate 3-hydroxylase (hpah) from acinetobacter baumannii
Analyse Crystal structure of the reductase (C1) component of P- hydroxyphenylacetate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZYR
- Type
- protein
- Length
- 612 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6Q271
- Ligands
- FMN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 306 | — | Q6Q271 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5ZYR · Crystal structure of the reductase (C1) component of p-hydroxyphenylacetate 3-hydroxylase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q6Q271 · AlphaFold monomer V2.0 prediction for P-hydroxyphenylacetate 3-hydroxylase, reductase… · a predicted model of the same protein · chain A against A, TM-score 0.66
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 Q6Q271
- Elsewhere: RCSB PDB 5ZYR · PDBe 5ZYR · UniProt Q6Q271
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