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Lipase II from rhizopus niveus

Analyse Lipase II from rhizopus niveus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LGY
Type: protein
Length: 795 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triacylglycerol lipase
EC: 3.1.1.3
UniProt: P61871
Pockets: 6 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Triacylglycerol lipase (EC 3.1.1.3)	protein	265	34% helix, 28% strand	P61871

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	285	0.49	0.73	35	empty
2	105	0.43	0.78	21	empty
3	99	0.42	0.78	16	empty
4	62	0.37	0.79	12	empty
5	79	0.36	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 51 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

1LGY · Lipase II from rhizopus niveus · the same entry in another collection · chain A against A, TM-score 1.00
P61871 · AlphaFold monomer V2.0 prediction for lipase (P61871) · 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 P61871
Elsewhere: RCSB PDB 1LGY · PDBe 1LGY · UniProt P61871

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