MolNFT v1 · #129485 · protein

The crystal structure of a highly thermostable carboxyl esterase from bacillus coagulans in complex with glycerol

5OLU · ALPHA/BETA hydrolase family protein: “The crystal structure of a highly thermostable carboxyl esterase from bacillus coagulans in complex with…”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.40). MolNFT v1 #129485…

PDB: 5OLU
Type: protein
Length: 310 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALPHA/BETA hydrolase family protein
UniProt: A0A0B5WSQ6
Ligands: CL
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALPHA/BETA hydrolase family protein	protein	310	42% helix, 16% strand	A0A0B5WSQ6

Ligands and binding sites

CL · Chloride ion · ion · 8 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.40	0.78	16	empty

Compared structures

5OLU · The crystal structure of a highly thermostable carboxyl esterase from Bacillus coagulans… · 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 A0A0B5WSQ6
Elsewhere: RCSB PDB 5OLU · PDBe 5OLU · UniProt A0A0B5WSQ6

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