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Structure of 6B, a thermostable mutant of bacillus subtilis lipase obtained through directed evolution

Analyse Structure of 6B, a thermostable mutant of bacillus subtilis lipase obtained… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3QMM
Type: protein
Length: 358 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase esta
EC: 3.1.1.3
UniProt: P37957
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lipase esta (EC 3.1.1.3)	protein	179	42% helix, 20% strand	P37957

Pockets

2 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	306	0.68	0.82	37	empty
2	145	0.46	0.77	25	empty

Interfaces

1 interface between chains.

A–B · 574 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

3QMM · Structure of 6B, a thermostable mutant of Bacillus subtilis lipase obtained through… · the same entry in another collection · chain A against A, TM-score 1.00
P37957 · AlphaFold monomer V2.0 prediction for lipase esta (P37957) · a predicted model of the same protein · 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 P37957
Elsewhere: RCSB PDB 3QMM · PDBe 3QMM · UniProt P37957

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