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 | 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 | 0106276 | molecular_function | biliberdin reductase (NAD+) activity |
A | 0106277 | molecular_function | biliverdin reductase (NADP+) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 601 |
Chain | Residue |
A | GLY15 |
A | VAL16 |
A | SER43 |
A | ARG44 |
A | ARG45 |
A | LYS209 |
A | HOH1095 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 A 602 |
Chain | Residue |
A | ALA104 |
A | SER285 |
A | LYS289 |
A | NAD901 |
A | HOH1023 |
A | HOH1075 |
A | SER102 |
A | PHE103 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 604 |
Chain | Residue |
A | PHE151 |
A | ARG171 |
A | ARG224 |
A | NAD900 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAD A 900 |
Chain | Residue |
A | ARG18 |
A | ALA19 |
A | SER74 |
A | SER76 |
A | HIS79 |
A | GLU96 |
A | TYR97 |
A | PRO98 |
A | GLU123 |
A | LEU156 |
A | PHE161 |
A | SER167 |
A | PO4604 |
A | HOH1005 |
A | HOH1025 |
A | HOH1107 |
A | HOH1150 |
A | HOH1218 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NAD A 901 |
Chain | Residue |
A | MET2 |
A | ILE3 |
A | GLU66 |
A | PHE103 |
A | GLN107 |
A | LYS223 |
A | VAL245 |
A | GLN264 |
A | LYS289 |
A | GLN293 |
A | PO4602 |
A | HOH1052 |
A | HOH1091 |
A | HOH1178 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ARG18 | |
A | SER76 | |
A | TYR97 | |
A | SER167 | |
Chain | Residue | Details |
A | HIS279 | |
A | CYS280 | |
A | CYS291 | |
A | HIS292 | |
Chain | Residue | Details |
A | SER154 | |
Chain | Residue | Details |
A | THR173 | |
Chain | Residue | Details |
A | SER177 | |
Chain | Residue | Details |
A | LYS247 | |
A | LYS252 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1gcu |
Chain | Residue | Details |
A | TYR97 | |
A | GLU126 | |
A | SER170 | |
A | GLU123 | |
A | GLU96 | |
A | ARG171 | |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 566 |
Chain | Residue | Details |
A | GLU96 | electrostatic stabiliser |
A | TYR97 | electrostatic stabiliser, proton acceptor, proton donor |
A | GLU123 | electrostatic stabiliser |
A | GLU126 | electrostatic stabiliser |
A | SER170 | electrostatic stabiliser |
A | ARG171 | electrostatic stabiliser |