Research workbench
Replacement of catalytic histidine-195 of chloramphenicol acetyltransferase: evidence for a general base role for glutamate
Analyse Replacement of catalytic histidine-195 of chloramphenicol acetyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CIA
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00484
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 213 | — | P00484 |
Compared structures
- 1CIA · Replacement of catalytic histidine-195 of chloramphenicol acetyltransferase: evidence for… · 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 1CIA · PDBe 1CIA · UniProt P00484
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