1HLG
CRYSTAL STRUCTURE OF HUMAN GASTRIC LIPASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004806 | molecular_function | triacylglycerol lipase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006108 | biological_process | malate metabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006641 | biological_process | triglyceride metabolic process |
| A | 0008289 | molecular_function | lipid binding |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016298 | molecular_function | lipase activity |
| A | 0016615 | molecular_function | malate dehydrogenase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| B | 0004806 | molecular_function | triacylglycerol lipase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006108 | biological_process | malate metabolic process |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006641 | biological_process | triglyceride metabolic process |
| B | 0008289 | molecular_function | lipid binding |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016298 | molecular_function | lipase activity |
| B | 0016615 | molecular_function | malate dehydrogenase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PDB Data
| site_id | SA |
| Number of Residues | 3 |
| Details | ACTIVE SITE CHAIN A |
| Chain | Residue |
| A | SER153 |
| A | ASP324 |
| A | HIS353 |
| site_id | SB |
| Number of Residues | 3 |
| Details | ACTIVE SITE CHAIN B |
| Chain | Residue |
| B | SER153 |
| B | ASP324 |
| B | HIS353 |
Functional Information from PROSITE/UniProt
| site_id | PS00120 |
| Number of Residues | 10 |
| Details | LIPASE_SER Lipases, serine active site. LHYVGHSQGT |
| Chain | Residue | Details |
| A | LEU147-THR156 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 598 |
| Details | Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10358049","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"10358049","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10358049","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1azw |
| Chain | Residue | Details |
| A | HIS353 | |
| A | ASP324 | |
| A | SER153 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1azw |
| Chain | Residue | Details |
| B | HIS353 | |
| B | ASP324 | |
| B | SER153 |
