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The crystal structure of chloramphenicol acetyltransferase from vibrio fischeri ES114
Analyse The crystal structure of chloramphenicol acetyltransferase from vibrio fischeri… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UX9
- Type
- protein
- Length
- 862 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chloramphenicol acetyltransferase
- EC
- 2.3.1.28
- UniProt
- Q5DZD6
- Ligands
- MG, CL
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 215 | 22% helix, 19% strand | Q5DZD6 |
| D | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 217 | 26% helix, 18% strand | Q5DZD6 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 6 copies · chains A, B, C, D
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 6 copies · chains A, B, C, D
- ACT · Acetate ion · additive · 6 copies · chains A, B, C, D
- FMT · Formic acid · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 760 | 0.73 | 0.78 | 74 | MES, ACT, CL |
| 2 | 694 | 0.73 | 0.79 | 71 | MES, ACT, CL |
| 3 | 742 | 0.72 | 0.78 | 72 | MES, CL |
| 4 | 404 | 0.69 | 0.81 | 49 | empty |
| 5 | 154 | 0.46 | 0.76 | 24 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1635 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 1627 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 1576 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 28 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 21 modified (engineered).
Compared structures
- 5UX9 · The crystal structure of chloramphenicol acetyltransferase from Vibrio fischeri ES114 · 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 Q5DZD6
- Elsewhere: RCSB PDB 5UX9 · PDBe 5UX9 · UniProt Q5DZD6
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