1EX9
CRYSTAL STRUCTURE OF THE PSEUDOMONAS AERUGINOSA LIPASE COMPLEXED WITH RC-(RP,SP)-1,2-DIOCTYLCARBAMOYL-GLYCERO-3-O-OCTYLPHOSPHONATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004806 | molecular_function | triacylglycerol lipase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0015628 | biological_process | protein secretion by the type II secretion system |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016298 | molecular_function | lipase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0043952 | biological_process | protein transport by the Sec complex |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 286 |
| Chain | Residue |
| A | ASP209 |
| A | ASP253 |
| A | GLN257 |
| A | VAL258 |
| A | LEU261 |
| A | HOH470 |
| A | HOH483 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OCP A 382 |
| Chain | Residue |
| A | LEU17 |
| A | TYR27 |
| A | SER82 |
| A | HIS83 |
| A | SER112 |
| A | LEU159 |
| A | HIS251 |
| A | VAL258 |
| A | GLY15 |
| A | MET16 |
Functional Information from PROSITE/UniProt
| site_id | PS00120 |
| Number of Residues | 10 |
| Details | LIPASE_SER Lipases, serine active site. VNLIGHSHGG |
| Chain | Residue | Details |
| A | VAL76-GLY85 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 245 |
| Details | Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10893416","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1632642","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1EX9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"10893416","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1632642","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1EX9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10893416","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EX9","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 | ASP229 | |
| A | HIS251 | |
| A | SER82 |
