Research workbench
Structure of cati in complex with chloramphenicol
Analyse Structure of cati in complex with chloramphenicol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3U9F
- Type
- protein
- Length
- 3,840 residues
- Chains
- 18
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chloramphenicol acetyltransferase
- EC
- 2.3.1.28
- UniProt
- P62577
- Ligands
- CLM
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 8 distinct chains · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 215 | 29% helix, 31% strand | P62577 |
| C, J, K, L | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 216 | 27% helix, 30% strand | P62577 |
| D, F, M, O | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 211 | 29% helix, 29% strand | P62577 |
| E | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 207 | 29% helix, 31% strand | P62577 |
| G, R, S | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 214 | 29% helix, 30% strand | P62577 |
| H, I | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 213 | 30% helix, 29% strand | P62577 |
| N | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 212 | 29% helix, 30% strand | P62577 |
| P | Chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 215 | 27% helix, 31% strand | P62577 |
Ligands and binding sites
- CLM · Chloramphenicol · ligand · 18 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, R, S
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 773 | 0.78 | 0.81 | 77 | CLM |
| 2 | 603 | 0.78 | 0.83 | 71 | CLM |
| 3 | 572 | 0.77 | 0.83 | 70 | CLM |
| 4 | 552 | 0.77 | 0.83 | 65 | CLM |
| 5 | 633 | 0.77 | 0.82 | 75 | CLM |
Interfaces
34 interfaces between chains.
- G–H · 1174 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 1154 Ų buried · 22 hydrogen bonds · protein-protein
- G–I · 1146 Ų buried · 18 hydrogen bonds · protein-protein
- K–L · 1146 Ų buried · 21 hydrogen bonds · protein-protein
- R–S · 1143 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 3U9F · Structure of CATI in complex with chloramphenicol · the same entry in another collection · chain K against K, 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 3U9F · PDBe 3U9F · UniProt P62577
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