Research workbench
Crystal structure of phenazine biosynthesis protein PHZA/B from burkholderia cepacia R18194, complex with 2- (CYCLOHEXYLAMINO)BENZOIC acid
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
- 3B4P
- 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
- 3B4, AZI
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenazine biosynthesis protein A/B | protein | 157 | 34% helix, 36% strand | Q396C9 |
| B | Phenazine biosynthesis protein A/B | protein | 158 | 34% helix, 36% strand | Q396C9 |
Ligands and binding sites
- 3B4 · 2-(cyclohexylamino)benzoic acid · ligand · 2 copies · chains A, B
- AZI · Azide ion · ion · chains A
- ACT · Acetate ion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.84 | 0.96 | 30 | 3B4, ACT |
| 2 | 195 | 0.83 | 0.97 | 31 | 3B4, AZI |
| 3 | 140 | 0.54 | 0.81 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 2242 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 3B4P · 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 3B4P · PDBe 3B4P · UniProt Q396C9
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