MolNFT v1 · #18860 · protein
Crystal structure of chloramphenicol acetyltransferase I complexed with fusidic acid at 2.18 a resolution
1Q23: “Crystal structure of chloramphenicol acetyltransferase I complexed with fusidic acid at 2.18 a resolution”. X-ray diffraction, 2 ligands (FUA, CA), 20 pockets (best druggability 0.79). MolNFT v1 #18860 on GenesisL1: 3D structure…
- PDB
- 1Q23
- Type
- protein
- Length
- 2,563 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chloramphenicol acetyltransferase
- EC
- 2.3.1.28
- UniProt
- P62577
- Ligands
- FUA, CA
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 9 distinct chains · 31% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 214 | 31% helix, 31% strand | P62577 |
| B | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 217 | 30% helix, 31% strand | P62577 |
| C, D, G | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 213 | 32% helix, 31% strand | P62577 |
| E, I | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 215 | 30% helix, 31% strand | P62577 |
| F | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 212 | 32% helix, 31% strand | P62577 |
| H | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 216 | 31% helix, 31% strand | P62577 |
| J | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 212 | 30% helix, 32% strand | P62577 |
| K | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 213 | 32% helix, 31% strand | P62577 |
| L | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 210 | 30% helix, 30% strand | P62577 |
Ligands and binding sites
- FUA · Fusidic acid · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 970 | 0.79 | 0.81 | 84 | FUA |
| 2 | 651 | 0.78 | 0.83 | 67 | FUA |
| 3 | 713 | 0.78 | 0.82 | 70 | FUA |
| 4 | 645 | 0.78 | 0.83 | 70 | FUA |
| 5 | 699 | 0.78 | 0.82 | 70 | FUA |
Interfaces
17 interfaces between chains.
- B–C · 1156 Ų buried · 23 hydrogen bonds · protein-protein
- G–I · 1151 Ų buried · 18 hydrogen bonds · protein-protein
- D–F · 1148 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1139 Ų buried · 17 hydrogen bonds · protein-protein
- D–E · 1138 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 1Q23 · Crystal structure of Chloramphenicol acetyltransferase I complexed with Fusidic acid at… · the same entry in another collection · chain L against L, 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 P62577
- Elsewhere: RCSB PDB 1Q23 · PDBe 1Q23 · UniProt P62577
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