Research workbench
Crystal structure of chloramphenicol acetyltransferase VCA0300 from vibrio cholerae O1 biovar eltor
Analyse Crystal structure of chloramphenicol acetyltransferase VCA0300 from vibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EEV
- Type
- protein
- Length
- 620 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chloramphenicol acetyltransferase
- UniProt
- Q9KMN1
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 3 distinct chains · 24% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chloramphenicol acetyltransferase | protein | 207 | 25% helix, 19% strand | Q9KMN1 |
| B | Chloramphenicol acetyltransferase | protein | 205 | 24% helix, 20% strand | Q9KMN1 |
| C | Chloramphenicol acetyltransferase | protein | 208 | 25% helix, 19% strand | Q9KMN1 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 434 | 0.72 | 0.82 | 46 | empty |
| 2 | 547 | 0.71 | 0.80 | 57 | MPD |
| 3 | 543 | 0.71 | 0.80 | 53 | MPD |
| 4 | 522 | 0.70 | 0.79 | 53 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1721 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1710 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 1685 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 3EEV · Crystal Structure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1… · the same entry in another collection · chain C against C, 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 Q9KMN1
- Elsewhere: RCSB PDB 3EEV · PDBe 3EEV · UniProt Q9KMN1
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