Research workbench
Acinetobacter baumannii P-hydroxyphenylacetate 3-hydroxylase (hpah), reductase component (C1)
Analyse Acinetobacter baumannii P-hydroxyphenylacetate 3-hydroxylase (hpah), reductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZC2
- Type
- protein
- Length
- 596 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P-hydroxyphenylacetate 3-hydroxylase, reductase component
- EC
- 1.5.1.36
- UniProt
- Q6Q271
- Ligands
- FMN
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | P-hydroxyphenylacetate 3-hydroxylase, reductase component (EC 1.5.1.36) | protein | 301 | 38% helix, 26% strand | Q6Q271 |
| A | P-hydroxyphenylacetate 3-hydroxylase, reductase component (EC 1.5.1.36) | protein | 295 | 40% helix, 26% strand | 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.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 693 | 0.79 | 0.84 | 60 | FMN |
| 2 | 692 | 0.78 | 0.83 | 67 | FMN |
| 3 | 89 | 0.76 | 0.98 | 28 | empty |
| 4 | 84 | 0.74 | 0.97 | 27 | empty |
| 5 | 293 | 0.53 | 0.75 | 47 | empty |
Interfaces
1 interface between chains.
- B–A · 5771 Ų buried · 63 hydrogen bonds · protein-protein
Compared structures
- 5ZC2 · Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component… · the same entry in another collection · chain B against B, 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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