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Wild-type bacillus subtilis lipase a with 5% [BMIM][CL]

Analyse Wild-type bacillus subtilis lipase a with 5% [BMIM][CL] in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CT4
Type: protein
Length: 359 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
EC: 3.1.1.3
UniProt: I6V559
Ligands: BM0, SO4, CL
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase (EC 3.1.1.3)	protein	179	42% helix, 20% strand	I6V559
B	Esterase (EC 3.1.1.3)	protein	180	40% helix, 19% strand	I6V559

Ligands and binding sites

BM0 · 1-butyl-3-methyl-1H-imidazol-3-ium · ligand · 2 copies · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A, B
CL · Chloride ion · ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	388	0.54	0.73	42	empty

Interfaces

1 interface between chains.

A–B · 135 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5CT4 · Wild-type Bacillus subtilis lipase A with 5% [BMIM][Cl] · 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 I6V559
Elsewhere: RCSB PDB 5CT4 · PDBe 5CT4 · UniProt I6V559

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