Research workbench
Crystal structure of bleomycin N-acetyltransferase complexed with coenzyme a in the orthorhombic crystal
Analyse Crystal structure of bleomycin N-acetyltransferase complexed with coenzyme a in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZW4
- Type
- protein
- Length
- 1,174 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bleomycin acetyltransferase
- UniProt
- Q53796
- Ligands
- COA, SO4
- Pockets
- 16 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bleomycin acetyltransferase | protein | 294 | 25% helix, 34% strand | Q53796 |
| C, D | Bleomycin acetyltransferase | protein | 293 | 26% helix, 33% strand | Q53796 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, C
- SO4 · Sulfate ion · ion · 9 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1101 | 0.81 | 0.82 | 91 | SO4 |
| 2 | 966 | 0.80 | 0.81 | 90 | SO4 |
| 3 | 744 | 0.78 | 0.82 | 91 | SO4 |
| 4 | 596 | 0.76 | 0.82 | 69 | SO4 |
| 5 | 416 | 0.75 | 0.85 | 51 | COA |
Interfaces
5 interfaces between chains.
- C–D · 2459 Ų buried · 31 hydrogen bonds · protein-protein
- A–B · 2452 Ų buried · 30 hydrogen bonds · protein-protein
- A–D · 478 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 334 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 10 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 2ZW4 · Crystal structure of bleomycin N-acetyltransferase complexed with coenzyme A in the… · 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 Q53796
- Elsewhere: RCSB PDB 2ZW4 · PDBe 2ZW4 · UniProt Q53796
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