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Crystal structure of human gastric lipase

Analyse Crystal structure of human gastric lipase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HLG
Type: protein
Length: 736 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase, gastric
EC: 3.1.1.3
UniProt: P07098
Ligands: NAG
Pockets: 10 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lipase, gastric (EC 3.1.1.3)	protein	368	42% helix, 15% strand	P07098

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	172	0.50	0.78	19	empty
2	101	0.50	0.81	16	empty
3	81	0.47	0.82	14	empty
4	112	0.46	0.79	19	empty
5	134	0.42	0.75	24	empty

Interfaces

1 interface between chains.

A–B · 413 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 glycan, 2 disulfide (N-glycosylation, disulfide).

Compared structures

1HLG · Crystal structure of human gastric lipase · the same entry in another collection · chain B against B, TM-score 1.00
P07098 · AlphaFold monomer V2.0 prediction for gastric triacylglycerol lipase (P07098) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P07098
Elsewhere: RCSB PDB 1HLG · PDBe 1HLG · UniProt P07098

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