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Chloramphenicol acetyltransferase

Analyse Chloramphenicol acetyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2I9D
Type: protein
Length: 600 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chloramphenicol acetyltransferase
UniProt: Q8A336
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chloramphenicol acetyltransferase	protein	214	34% helix, 28% strand	Q8A336
B, C	Chloramphenicol acetyltransferase	protein	193	34% helix, 30% strand	Q8A336

Pockets

6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	99	0.77	0.98	29	empty
2	368	0.75	0.85	57	empty
3	358	0.70	0.82	42	empty
4	382	0.68	0.80	37	empty
5	387	0.66	0.80	41	empty

Interfaces

3 interfaces between chains.

A–B · 1260 Å² buried · 19 hydrogen bonds · protein-protein
A–C · 909 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 864 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

2I9D · chloramphenicol acetyltransferase · 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 Q8A336
Elsewhere: RCSB PDB 2I9D · PDBe 2I9D · UniProt Q8A336

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