MolNFT v2 · #142451 · protein
Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component (C1)
5ZC2: “Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component (C1)”. X-ray diffraction at 2.898, 1 ligand (FMN). MolNFT v2 #142451 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5ZC2
- Type
- protein
- Length
- 596 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.898
- Source
- Acinetobacter baumannii
- UniProt
- Q6Q271
- Ligands
- FMN
Structure
x-ray diffraction · resolution 2.898 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 301 | — | Q6Q271 |
| A | — | protein | 295 | — | Q6Q271 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5ZC2 · Acinetobacter baumannii P-hydroxyphenylacetate 3-hydroxylase (hpah), reductase component… · 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 5ZC2 · PDBe 5ZC2 · UniProt Q6Q271
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