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Structure of the bacillus stearothermophilus L1 lipase

Analyse Structure of the bacillus stearothermophilus L1 lipase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KU0
Type: protein
Length: 773 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L1 lipase
EC: 3.1.1.3
UniProt: O66015
Ligands: ZN, CA
Pockets: 6 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L1 lipase (EC 3.1.1.3)	protein	388	40% helix, 16% strand	O66015
B	L1 lipase (EC 3.1.1.3)	protein	385	37% helix, 15% strand	O66015

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	324	0.60	0.78	41	empty
2	350	0.57	0.76	33	empty
3	191	0.51	0.77	24	empty
4	67	0.41	0.81	20	empty
5	72	0.30	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 404 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

1KU0 · Structure of the Bacillus stearothermophilus L1 lipase · 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 O66015
Elsewhere: RCSB PDB 1KU0 · PDBe 1KU0 · UniProt O66015

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