1VBJ
The crystal structure of prostaglandin F synthase from Trypanosoma brucei
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001516 | biological_process | prostaglandin biosynthetic process |
| A | 0004033 | molecular_function | obsolete aldo-keto reductase (NADPH) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0019571 | biological_process | D-arabinose catabolic process |
| A | 0045290 | molecular_function | D-arabinose 1-dehydrogenase [NAD(P)+] activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0001516 | biological_process | prostaglandin biosynthetic process |
| B | 0004033 | molecular_function | obsolete aldo-keto reductase (NADPH) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0019571 | biological_process | D-arabinose catabolic process |
| B | 0045290 | molecular_function | D-arabinose 1-dehydrogenase [NAD(P)+] activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP A 3001 |
| Chain | Residue |
| A | GLY21 |
| A | GLN161 |
| A | TRP187 |
| A | SER188 |
| A | PRO189 |
| A | LEU190 |
| A | GLY191 |
| A | GLN192 |
| A | GLY193 |
| A | VAL196 |
| A | ALA213 |
| A | MET22 |
| A | ILE228 |
| A | PRO229 |
| A | LYS230 |
| A | SER231 |
| A | GLY232 |
| A | ARG236 |
| A | GLU239 |
| A | ASN240 |
| A | CIT4001 |
| A | HOH4024 |
| A | TRP23 |
| A | HOH4026 |
| A | HOH4082 |
| A | HOH4126 |
| A | ASP47 |
| A | TYR52 |
| A | LYS77 |
| A | HIS110 |
| A | SER139 |
| A | ASN140 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAP B 3002 |
| Chain | Residue |
| B | GLY21 |
| B | MET22 |
| B | TRP23 |
| B | ASP47 |
| B | TYR52 |
| B | LYS77 |
| B | HIS110 |
| B | SER139 |
| B | ASN140 |
| B | GLN161 |
| B | TRP187 |
| B | SER188 |
| B | PRO189 |
| B | LEU190 |
| B | GLY191 |
| B | GLN192 |
| B | GLY193 |
| B | VAL196 |
| B | ALA213 |
| B | ILE228 |
| B | PRO229 |
| B | LYS230 |
| B | SER231 |
| B | GLY232 |
| B | ARG236 |
| B | GLU239 |
| B | ASN240 |
| B | CIT4002 |
| B | HOH4074 |
| B | HOH4128 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CIT A 4001 |
| Chain | Residue |
| A | TRP23 |
| A | ILE51 |
| A | TYR52 |
| A | TRP79 |
| A | HIS110 |
| A | TRP111 |
| A | LYS131 |
| A | NAP3001 |
| A | HOH4249 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CIT B 4002 |
| Chain | Residue |
| B | TRP23 |
| B | TYR52 |
| B | TRP79 |
| B | HIS110 |
| B | TRP111 |
| B | TRP187 |
| B | GLY266 |
| B | PRO267 |
| B | PHE272 |
| B | NAP3002 |
| B | HOH4153 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. FeklyadkkVRAIGVSNF |
| Chain | Residue | Details |
| A | PHE124-PHE141 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDTAaiyknEesAG |
| Chain | Residue | Details |
| A | GLY42-GLY59 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2004","submissionDatabase":"PDB data bank","title":"The crystal structure of prostaglandin F synthase from Trypanosoma brucei.","authors":["Inoue T."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | ASP47 | |
| A | TYR52 | |
| A | HIS110 | |
| A | LYS77 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | ASP47 | |
| B | TYR52 | |
| B | HIS110 | |
| B | LYS77 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | TYR52 | |
| A | LYS77 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| B | TYR52 | |
| B | LYS77 |
