MolNFT v1 · #80852 · protein

Structure of cati in complex with chloramphenicol

3U9F · Chloramphenicol acetyltransferase: “Structure of cati in complex with chloramphenicol”. X-ray diffraction, 1 ligand (CLM), 20 pockets (best druggability 0.78). MolNFT v1 #80852 on GenesisL1: 3D structure, binding sites and pockets…

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.

Pocket	Volume (Å³)	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 Å² buried · 22 hydrogen bonds · protein-protein
E–F · 1154 Å² buried · 22 hydrogen bonds · protein-protein
G–I · 1146 Å² buried · 18 hydrogen bonds · protein-protein
K–L · 1146 Å² buried · 21 hydrogen bonds · protein-protein
R–S · 1143 Å² 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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