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Crystal structure of phenazine biosynthesis protein PHZA/B from burkholderia cepacia R18194, dhha complex
Analyse Crystal structure of phenazine biosynthesis protein PHZA/B from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CNM
- Type
- protein
- Length
- 315 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenazine biosynthesis protein A/B
- UniProt
- Q396C9
- Ligands
- HHA
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenazine biosynthesis protein A/B | protein | 157 | 34% helix, 35% strand | Q396C9 |
| B | Phenazine biosynthesis protein A/B | protein | 158 | 34% helix, 35% strand | Q396C9 |
Ligands and binding sites
- HHA · (2S,3S)-trans-2,3-dihydro-3-hydroxyanthranilic acid · ligand · 2 copies · chains A, B
- ACT · Acetate ion · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 207 | 0.83 | 0.96 | 35 | HHA, ACT |
| 2 | 193 | 0.83 | 0.96 | 33 | ACT, HHA |
| 3 | 92 | 0.48 | 0.81 | 24 | empty |
| 4 | 53 | 0.36 | 0.80 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 2267 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 3CNM · Crystal Structure of Phenazine Biosynthesis Protein PhzA/B from Burkholderia cepacia… · 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 Q396C9
- Elsewhere: RCSB PDB 3CNM · PDBe 3CNM · UniProt Q396C9
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