1V3V
Crystal structure of leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase complexed with NADP and 15-oxo-PGE2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| 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)+] activity |
| A | 0035798 | molecular_function | 2-alkenal reductase (NADPH) activity |
| A | 0036102 | biological_process | leukotriene B4 metabolic process |
| A | 0036132 | molecular_function | 13-prostaglandin reductase activity |
| A | 0036185 | molecular_function | 13-lipoxin reductase activity |
| A | 0047522 | molecular_function | 15-oxoprostaglandin 13-oxidase 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 | 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)+] activity |
| B | 0035798 | molecular_function | 2-alkenal reductase (NADPH) activity |
| B | 0036102 | biological_process | leukotriene B4 metabolic process |
| B | 0036132 | molecular_function | 13-prostaglandin reductase activity |
| B | 0036185 | molecular_function | 13-lipoxin reductase activity |
| B | 0047522 | molecular_function | 15-oxoprostaglandin 13-oxidase 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 | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1001 |
| Chain | Residue |
| B | HIS12 |
| B | PHE13 |
| B | SER54 |
| B | LYS55 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 1002 |
| Chain | Residue |
| B | GLU315 |
| B | ASN318 |
| B | HOH2533 |
| B | HOH2552 |
| B | HOH2556 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 1003 |
| Chain | Residue |
| A | ASN318 |
| A | HOH1501 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1004 |
| Chain | Residue |
| A | HIS12 |
| A | PHE13 |
| A | SER54 |
| A | LYS55 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1005 |
| Chain | Residue |
| A | ARG51 |
| A | HOH1418 |
| A | HOH1760 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1006 |
| Chain | Residue |
| B | GLY15 |
| B | ARG51 |
| B | ASN246 |
| B | HOH2410 |
| site_id | AC7 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAP A 1350 |
| Chain | Residue |
| A | PRO48 |
| A | MET124 |
| A | THR128 |
| A | GLY152 |
| A | ALA153 |
| A | VAL154 |
| A | GLY174 |
| A | LYS178 |
| A | TYR193 |
| A | ASN217 |
| A | VAL218 |
| A | CYS239 |
| A | GLY240 |
| A | ILE242 |
| A | SER243 |
| A | TYR245 |
| A | PHE270 |
| A | ILE271 |
| A | VAL272 |
| A | MET316 |
| A | LEU317 |
| A | GLY319 |
| A | ASN321 |
| A | 5OP1360 |
| A | HOH1361 |
| A | HOH1363 |
| A | HOH1364 |
| A | HOH1366 |
| A | HOH1369 |
| A | HOH1401 |
| A | HOH1406 |
| A | HOH1426 |
| A | HOH1626 |
| A | HOH1632 |
| A | HOH1687 |
| site_id | AC8 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NAP B 2350 |
| Chain | Residue |
| B | PRO48 |
| B | MET124 |
| B | THR128 |
| B | GLY152 |
| B | ALA153 |
| B | VAL154 |
| B | ALA173 |
| B | GLY174 |
| B | LYS178 |
| B | TYR193 |
| B | ASN217 |
| B | VAL218 |
| B | CYS239 |
| B | GLY240 |
| B | ILE242 |
| B | SER243 |
| B | TYR245 |
| B | PHE270 |
| B | ILE271 |
| B | VAL272 |
| B | MET316 |
| B | LEU317 |
| B | GLY319 |
| B | ASN321 |
| B | 5OP2360 |
| B | HOH2366 |
| B | HOH2367 |
| B | HOH2368 |
| B | HOH2372 |
| B | HOH2379 |
| B | HOH2391 |
| B | HOH2475 |
| B | HOH2520 |
| B | HOH2522 |
| B | HOH2524 |
| B | HOH2603 |
| B | HOH2683 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 5OP A 1360 |
| Chain | Residue |
| B | GLU258 |
| B | ILE261 |
| B | TYR262 |
| A | TYR49 |
| A | TYR245 |
| A | TYR273 |
| A | NAP1350 |
| A | HOH1379 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 5OP B 2360 |
| Chain | Residue |
| A | GLU258 |
| A | ILE261 |
| A | TYR262 |
| B | TYR49 |
| B | TYR245 |
| B | TYR273 |
| B | NAP2350 |
| B | HOH2395 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15007077 |
| Chain | Residue | Details |
| A | GLY152 | |
| B | TYR193 | |
| B | ASN217 | |
| B | CYS239 | |
| B | PHE270 | |
| B | ASN321 | |
| A | LYS178 | |
| A | TYR193 | |
| A | ASN217 | |
| A | CYS239 | |
| A | PHE270 | |
| A | ASN321 | |
| B | GLY152 | |
| B | LYS178 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q14914 |
| Chain | Residue | Details |
| A | THR18 | |
| B | THR18 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q14914 |
| Chain | Residue | Details |
| A | SER20 | |
| B | SER20 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q91YR9 |
| Chain | Residue | Details |
| A | LYS178 | |
| B | LYS178 |
