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Crystal structure of chloramphenicol-metabolizaing enzyme ESTDL136

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: 6AAE
Type: protein
Length: 622 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
EC: 3.1.1.1
UniProt: G3CR02
Pockets: 3 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase (EC 3.1.1.1)	protein	308	40% helix, 17% strand	G3CR02
B	Esterase (EC 3.1.1.1)	protein	314	38% helix, 16% strand	G3CR02

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 13 copies · chains A, B
1PE · Pentaethylene glycol · additive · 6 copies · chains A, B

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	1158	0.87	0.88	103	1PE, PEG
2	155	0.45	0.76	24	empty
3	51	0.28	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 2288 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

6AAE · Crystal structure of Chloramphenicol-Metabolizaing Enzyme EstDL136 · 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 G3CR02
Elsewhere: RCSB PDB 6AAE · PDBe 6AAE · UniProt G3CR02

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