Research workbench
Evidence for transition-state stabilization by serine-148 in the catalytic mechanism of chloramphenicol acetyltransferase
Analyse Evidence for transition-state stabilization by serine-148 in the catalytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CLA
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type III chloramphenicol acetyltransferase
- EC
- 2.3.1.28
- UniProt
- P00484
- Ligands
- CLM, CO
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Type III chloramphenicol acetyltransferase (EC 2.3.1.28) | protein | 213 | 30% helix, 28% strand | P00484 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 269 | 0.54 | 0.76 | 44 | CLM |
Compared structures
- 1CLA · Evidence for transition-state stabilization by serine-148 in the catalytic mechanism of… · the same entry in another collection · chain A against A, TM-score 1.00
- P00484 · AlphaFold monomer V2.0 prediction for chloramphenicol acetyltransferase 3 (P00484) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00484
- Elsewhere: RCSB PDB 1CLA · PDBe 1CLA · UniProt P00484
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