1TAH
THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE
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 | 0006629 | biological_process | lipid metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004806 | molecular_function | triacylglycerol lipase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004806 | molecular_function | triacylglycerol lipase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0016042 | biological_process | lipid catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004806 | molecular_function | triacylglycerol lipase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0016042 | biological_process | lipid catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 320 |
| Chain | Residue |
| B | ASP241 |
| B | ASP287 |
| B | GLN291 |
| B | VAL295 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 320 |
| Chain | Residue |
| A | ASP241 |
| A | ASP287 |
| A | GLN291 |
| A | VAL295 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 320 |
| Chain | Residue |
| C | ASP241 |
| C | ASP287 |
| C | GLN291 |
| C | VAL295 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 320 |
| Chain | Residue |
| D | ASP241 |
| D | ASP287 |
| D | GLN291 |
| D | VAL295 |
| site_id | ACA |
| Number of Residues | 4 |
| Details | ACTIVE SITE |
| Chain | Residue |
| A | HIS285 |
| A | ASP263 |
| A | GLU288 |
| A | SER87 |
| site_id | ACB |
| Number of Residues | 4 |
| Details | ACTIVE SITE |
| Chain | Residue |
| B | SER87 |
| B | HIS285 |
| B | ASP263 |
| B | GLU288 |
| site_id | ACC |
| Number of Residues | 4 |
| Details | ACTIVE SITE |
| Chain | Residue |
| C | SER87 |
| C | HIS285 |
| C | ASP263 |
| C | GLU288 |
| site_id | ACD |
| Number of Residues | 4 |
| Details | ACTIVE SITE |
| Chain | Residue |
| D | SER87 |
| D | HIS285 |
| D | ASP263 |
| D | GLU288 |
| site_id | CAA |
| Number of Residues | 4 |
| Details | CALCIUM SITE NEAR TO THE ACTIVE SITE |
| Chain | Residue |
| A | ASP287 |
| A | GLN291 |
| A | ASP241 |
| A | VAL295 |
| site_id | CAB |
| Number of Residues | 4 |
| Details | CALCIUM SITE NEAR TO THE ACTIVE SITE |
| Chain | Residue |
| B | ASP287 |
| B | GLN291 |
| B | ASP241 |
| B | VAL295 |
| site_id | CAC |
| Number of Residues | 4 |
| Details | CALCIUM SITE NEAR TO THE ACTIVE SITE |
| Chain | Residue |
| C | ASP287 |
| C | GLN291 |
| C | ASP241 |
| C | VAL295 |
| site_id | CAD |
| Number of Residues | 4 |
| Details | CALCIUM SITE NEAR TO THE ACTIVE SITE |
| Chain | Residue |
| D | ASP287 |
| D | GLN291 |
| D | ASP241 |
| D | VAL295 |
Functional Information from PROSITE/UniProt
| site_id | PS00120 |
| Number of Residues | 10 |
| Details | LIPASE_SER Lipases, serine active site. VNLIGHSQGG |
| Chain | Residue | Details |
| B | VAL81-GLY90 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1116 |
| Details | Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"1476423","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8405390","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"1476423","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8405390","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P22088","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16518399","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8405390","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TAH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ES4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details |
| Chain | Residue | Details |
| B | HIS285 | |
| B | SER87 | |
| B | ASP263 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details |
| Chain | Residue | Details |
| A | HIS285 | |
| A | SER87 | |
| A | ASP263 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details |
| Chain | Residue | Details |
| C | HIS285 | |
| C | SER87 | |
| C | ASP263 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details |
| Chain | Residue | Details |
| D | HIS285 | |
| D | SER87 | |
| D | ASP263 |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 519 |
| Chain | Residue | Details |
| B | ASP56 | electrostatic stabiliser |
| B | VAL126 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | LEU127 | electrostatic stabiliser |
| B | SER280 | metal ligand |
| B | ASP302 | electrostatic stabiliser, increase basicity, modifies pKa |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 519 |
| Chain | Residue | Details |
| C | ASP56 | electrostatic stabiliser |
| C | VAL126 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | LEU127 | electrostatic stabiliser |
| C | SER280 | metal ligand |
| C | ASP302 | electrostatic stabiliser, increase basicity, modifies pKa |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 519 |
| Chain | Residue | Details |
| A | ASP56 | electrostatic stabiliser |
| A | VAL126 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | LEU127 | electrostatic stabiliser |
| A | SER280 | metal ligand |
| A | ASP302 | electrostatic stabiliser, increase basicity, modifies pKa |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 519 |
| Chain | Residue | Details |
| D | ASP56 | electrostatic stabiliser |
| D | VAL126 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | LEU127 | electrostatic stabiliser |
| D | SER280 | metal ligand |
| D | ASP302 | electrostatic stabiliser, increase basicity, modifies pKa |
