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Crystal structure of chloramphenicol-metabolizaing enzyme ESTDL136- chloramphenicol complex

Analyse Crystal structure of chloramphenicol-metabolizaing enzyme ESTDL136… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IEY
Type: protein
Length: 616 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
EC: 3.1.1.1
UniProt: G3CR02
Ligands: CLM
Pockets: 3 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Esterase (EC 3.1.1.1)	protein	309	40% helix, 19% strand	G3CR02
A	Esterase (EC 3.1.1.1)	protein	307	39% helix, 16% strand	G3CR02

Ligands and binding sites

CLM · Chloramphenicol · ligand · chains B, A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1157	0.86	0.87	106	CLM
2	150	0.42	0.75	27	empty
3	89	0.36	0.75	15	empty

Interfaces

1 interface between chains.

B–A · 2275 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

6IEY · Crystal structure of Chloramphenicol-Metabolizaing Enzyme EstDL136-Chloramphenicol complex · the same entry in another collection · chain B against B, TM-score 1.00

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Every structure of UniProt G3CR02
Elsewhere: RCSB PDB 6IEY · PDBe 6IEY · UniProt G3CR02

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