MolNFT v1 · #137870 · protein

Culex quinquefasciatus carboxylesterase B2

5W1U · Carboxylic ester hydrolase: “Culex quinquefasciatus carboxylesterase B2”. X-ray diffraction, 4 pockets (best druggability 0.82). MolNFT v1 #137870 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5W1U
Type: protein
Length: 1,073 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxylic ester hydrolase
EC: 3.1.1.-
UniProt: Q23734
Pockets: 4 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxylic ester hydrolase (EC 3.1.1.-)	protein	536	34% helix, 18% strand	Q23734
B	Carboxylic ester hydrolase (EC 3.1.1.-)	protein	537	35% helix, 16% strand	Q23734

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B
MLI · Malonate ion · additive · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1112	0.82	0.83	88	EPE, MLI
2	938	0.80	0.82	66	EPE, MLI
3	798	0.78	0.82	72	empty
4	347	0.67	0.81	38	empty

Interfaces

1 interface between chains.

A–B · 732 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5W1U · Culex quinquefasciatus carboxylesterase B2 · the same entry in another collection · chain B against B, 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 Q23734
Elsewhere: RCSB PDB 5W1U · PDBe 5W1U · UniProt Q23734

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