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 | aldo-keto reductase (NADPH) activity |
A | 0005737 | cellular_component | cytoplasm |
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 | 0036130 | molecular_function | prostaglandin H2 endoperoxidase reductase activity |
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 | aldo-keto reductase (NADPH) activity |
B | 0005737 | cellular_component | cytoplasm |
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 | 0036130 | molecular_function | prostaglandin H2 endoperoxidase reductase activity |
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 | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | TYR52 | |
B | TYR52 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|Ref.2 |
Chain | Residue | Details |
A | MET22 | |
B | SER139 | |
B | GLN161 | |
B | TRP187 | |
B | LYS230 | |
B | ARG236 | |
A | ASP47 | |
A | SER139 | |
A | GLN161 | |
A | TRP187 | |
A | LYS230 | |
A | ARG236 | |
B | MET22 | |
B | ASP47 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS110 | |
B | HIS110 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Lowers pKa of active site Tyr => ECO:0000250 |
Chain | Residue | Details |
A | LYS77 | |
B | LYS77 |
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 |