1V3U
Crystal structure of leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase in apo form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006693 | biological_process | prostaglandin metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
A | 0032440 | molecular_function | 2-alkenal reductase [NAD(P)H] activity |
A | 0035798 | molecular_function | 2-alkenal reductase (NADPH) activity |
A | 0036102 | biological_process | leukotriene B4 metabolic process |
A | 0036185 | molecular_function | 13-lipoxin reductase activity |
A | 0047522 | molecular_function | 15-oxoprostaglandin 13-reductase [NAD(P)+] activity |
A | 0097257 | molecular_function | leukotriene B4 12-hydroxy dehydrogenase activity |
A | 2001302 | biological_process | lipoxin A4 metabolic process |
B | 0005737 | cellular_component | cytoplasm |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006693 | biological_process | prostaglandin metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
B | 0032440 | molecular_function | 2-alkenal reductase [NAD(P)H] activity |
B | 0035798 | molecular_function | 2-alkenal reductase (NADPH) activity |
B | 0036102 | biological_process | leukotriene B4 metabolic process |
B | 0036185 | molecular_function | 13-lipoxin reductase activity |
B | 0047522 | molecular_function | 15-oxoprostaglandin 13-reductase [NAD(P)+] activity |
B | 0097257 | molecular_function | leukotriene B4 12-hydroxy dehydrogenase activity |
B | 2001302 | biological_process | lipoxin A4 metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 1001 |
Chain | Residue |
A | LYS324 |
A | ALA325 |
A | HOH1045 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CL B 1002 |
Chain | Residue |
B | HOH1119 |
B | ALA149 |
B | ALA151 |
B | ALA173 |
B | GLY174 |
B | LYS178 |
B | HOH1106 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 1003 |
Chain | Residue |
B | HIS12 |
B | PHE13 |
B | SER54 |
B | LYS55 |
B | HOH1126 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 1004 |
Chain | Residue |
A | ARG70 |
A | VAL72 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 1005 |
Chain | Residue |
B | ASN321 |
B | LYS324 |
B | ALA325 |
B | HOH1027 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 1006 |
Chain | Residue |
A | ALA149 |
A | ALA151 |
A | ALA173 |
A | LYS178 |
A | HOH1257 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 1007 |
Chain | Residue |
B | HIS12 |
B | GLU59 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15007077","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q14914","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q14914","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91YR9","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |