2H63
Crystal Structure of Human Biliverdin Reductase A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004074 | molecular_function | biliverdin reductase [NAD(P)+] activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042167 | biological_process | heme catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0106276 | molecular_function | biliberdin reductase (NAD+) activity |
| A | 0106277 | molecular_function | biliverdin reductase (NADP+) activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004074 | molecular_function | biliverdin reductase [NAD(P)+] activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042167 | biological_process | heme catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0106276 | molecular_function | biliberdin reductase (NAD+) activity |
| B | 0106277 | molecular_function | biliverdin reductase (NADP+) activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004074 | molecular_function | biliverdin reductase [NAD(P)+] activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042167 | biological_process | heme catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 0106276 | molecular_function | biliberdin reductase (NAD+) activity |
| C | 0106277 | molecular_function | biliverdin reductase (NADP+) activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004074 | molecular_function | biliverdin reductase [NAD(P)+] activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042167 | biological_process | heme catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070062 | cellular_component | extracellular exosome |
| D | 0106276 | molecular_function | biliberdin reductase (NAD+) activity |
| D | 0106277 | molecular_function | biliverdin reductase (NADP+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAP A 501 |
| Chain | Residue |
| A | GLY15 |
| A | SER75 |
| A | SER77 |
| A | HIS80 |
| A | GLU97 |
| A | TYR98 |
| A | PHE162 |
| D | SER235 |
| A | VAL16 |
| A | GLY17 |
| A | ARG18 |
| A | ALA19 |
| A | SER44 |
| A | ARG45 |
| A | ARG46 |
| A | CYS74 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAP B 501 |
| Chain | Residue |
| B | GLY15 |
| B | VAL16 |
| B | GLY17 |
| B | ARG18 |
| B | ALA19 |
| B | SER44 |
| B | ARG45 |
| B | ARG46 |
| B | CYS74 |
| B | SER75 |
| B | SER77 |
| B | HIS80 |
| B | GLU97 |
| B | TYR98 |
| B | PHE162 |
| B | PHE251 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAP C 501 |
| Chain | Residue |
| C | GLY15 |
| C | VAL16 |
| C | GLY17 |
| C | ARG18 |
| C | ALA19 |
| C | SER44 |
| C | ARG45 |
| C | ARG46 |
| C | CYS74 |
| C | SER75 |
| C | SER77 |
| C | HIS80 |
| C | GLU97 |
| C | TYR98 |
| C | GLU124 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP D 501 |
| Chain | Residue |
| A | ARG7 |
| C | SER235 |
| D | GLY15 |
| D | VAL16 |
| D | GLY17 |
| D | ARG18 |
| D | ALA19 |
| D | SER44 |
| D | ARG45 |
| D | ARG46 |
| D | CYS74 |
| D | SER75 |
| D | SER77 |
| D | HIS80 |
| D | GLU97 |
| D | TYR98 |
| D | GLU124 |
| D | PHE162 |
| D | HOH507 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|Ref.19, ECO:0007744|PDB:2H63 |
| Chain | Residue | Details |
| A | VAL16 | |
| C | SER44 | |
| C | SER77 | |
| C | TYR98 | |
| D | VAL16 | |
| D | SER44 | |
| D | SER77 | |
| D | TYR98 | |
| A | SER44 | |
| A | SER77 | |
| A | TYR98 | |
| B | VAL16 | |
| B | SER44 | |
| B | SER77 | |
| B | TYR98 | |
| C | VAL16 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000303|PubMed:8631357 |
| Chain | Residue | Details |
| A | HIS280 | |
| C | CYS281 | |
| C | CYS292 | |
| C | CYS293 | |
| D | HIS280 | |
| D | CYS281 | |
| D | CYS292 | |
| D | CYS293 | |
| A | CYS281 | |
| A | CYS292 | |
| A | CYS293 | |
| B | HIS280 | |
| B | CYS281 | |
| B | CYS292 | |
| B | CYS293 | |
| C | HIS280 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | THR174 | |
| B | THR174 | |
| C | THR174 | |
| D | THR174 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | SER178 | |
| B | SER178 | |
| C | SER178 | |
| D | SER178 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | SER230 | |
| B | SER230 | |
| C | SER230 | |
| D | SER230 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS248 | |
| A | LYS253 | |
| B | LYS248 | |
| B | LYS253 | |
| C | LYS248 | |
| C | LYS253 | |
| D | LYS248 | |
| D | LYS253 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1gcu |
| Chain | Residue | Details |
| A | ARG172 | |
| A | GLU97 | |
| A | TYR98 | |
| A | GLU124 | |
| A | GLU127 | |
| A | SER171 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1gcu |
| Chain | Residue | Details |
| B | ARG172 | |
| B | GLU97 | |
| B | TYR98 | |
| B | GLU124 | |
| B | GLU127 | |
| B | SER171 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1gcu |
| Chain | Residue | Details |
| C | ARG172 | |
| C | GLU97 | |
| C | TYR98 | |
| C | GLU124 | |
| C | GLU127 | |
| C | SER171 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1gcu |
| Chain | Residue | Details |
| D | ARG172 | |
| D | GLU97 | |
| D | TYR98 | |
| D | GLU124 | |
| D | GLU127 | |
| D | SER171 |
