2ES4
Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate 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 | 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 |
| D | 0006457 | biological_process | protein folding |
| D | 0016020 | cellular_component | membrane |
| D | 0051082 | molecular_function | unfolded protein binding |
| E | 0006457 | biological_process | protein folding |
| E | 0016020 | cellular_component | membrane |
| E | 0051082 | molecular_function | unfolded protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 999 |
| Chain | Residue |
| A | ASP241 |
| A | ASP287 |
| A | GLN291 |
| A | LEU292 |
| A | VAL295 |
| A | HOH1056 |
| A | HOH1064 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 998 |
| Chain | Residue |
| B | GLN291 |
| B | LEU292 |
| B | VAL295 |
| B | HOH1066 |
| B | HOH1087 |
| B | ASP241 |
| B | ASP287 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IOD B 903 |
| Chain | Residue |
| B | GLN34 |
| B | VAL46 |
| B | HOH1075 |
| E | GLN234 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IOD B 904 |
| Chain | Residue |
| B | GLU197 |
| B | HOH1266 |
| E | GLN256 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD B 906 |
| Chain | Residue |
| B | GLY188 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD B 907 |
| Chain | Residue |
| B | GLN261 |
Functional Information from PROSITE/UniProt
| site_id | PS00120 |
| Number of Residues | 10 |
| Details | LIPASE_SER Lipases, serine active site. VNLIGHSQGG |
| Chain | Residue | Details |
| A | VAL81-GLY90 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| 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_FI2 |
| Number of Residues | 4 |
| 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_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P22088","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| 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 | Annotated By Reference To The Literature 1tah |
| Chain | Residue | Details |
| A | HIS285 | |
| A | SER87 | |
| A | ASP263 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1tah |
| Chain | Residue | Details |
| B | HIS285 | |
| B | SER87 | |
| B | ASP263 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1tah |
| Chain | Residue | Details |
| A | LEU17 | |
| A | HIS285 | |
| A | GLN88 | |
| A | SER87 | |
| A | ASP263 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1tah |
| Chain | Residue | Details |
| B | LEU17 | |
| B | HIS285 | |
| B | GLN88 | |
| B | SER87 | |
| B | ASP263 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 519 |
| Chain | Residue | Details |
| A | LEU17 | electrostatic stabiliser |
| A | SER87 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLN88 | electrostatic stabiliser |
| A | ASP241 | metal ligand |
| A | ASP263 | electrostatic stabiliser, increase basicity, modifies pKa |
| A | HIS285 | proton acceptor, proton donor |
| A | ASP287 | metal ligand |
| A | GLN291 | metal ligand |
| A | VAL295 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 519 |
| Chain | Residue | Details |
