7ER7
Crystal structure of hyman Biliverdin IX-beta reductase B with Tamibarotene (A80)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004074 | molecular_function | biliverdin reductase [NAD(P)+] activity |
A | 0005515 | molecular_function | protein binding |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0030219 | biological_process | megakaryocyte differentiation |
A | 0035605 | molecular_function | peptidyl-cysteine S-nitrosylase activity |
A | 0042167 | biological_process | heme catabolic process |
A | 0042602 | molecular_function | riboflavin reductase (NADPH) activity |
A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
A | 0046627 | biological_process | negative regulation of insulin receptor signaling pathway |
A | 0052873 | molecular_function | FMN reductase (NADPH) activity |
A | 0052874 | molecular_function | FMN reductase (NADH) activity |
A | 0070062 | cellular_component | extracellular exosome |
B | 0003824 | molecular_function | catalytic activity |
B | 0004074 | molecular_function | biliverdin reductase [NAD(P)+] activity |
B | 0005515 | molecular_function | protein binding |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0030219 | biological_process | megakaryocyte differentiation |
B | 0035605 | molecular_function | peptidyl-cysteine S-nitrosylase activity |
B | 0042167 | biological_process | heme catabolic process |
B | 0042602 | molecular_function | riboflavin reductase (NADPH) activity |
B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
B | 0046627 | biological_process | negative regulation of insulin receptor signaling pathway |
B | 0052873 | molecular_function | FMN reductase (NADPH) activity |
B | 0052874 | molecular_function | FMN reductase (NADH) activity |
B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 36 |
Details | binding site for residue NAP A 401 |
Chain | Residue |
A | GLY10 |
A | LEU74 |
A | LEU75 |
A | GLY76 |
A | ARG78 |
A | VAL86 |
A | MET87 |
A | CYS109 |
A | THR110 |
A | HIS132 |
A | PRO151 |
A | THR12 |
A | PRO152 |
A | HIS153 |
A | ILE154 |
A | A80402 |
A | HOH508 |
A | HOH515 |
A | HOH528 |
A | HOH548 |
A | HOH556 |
A | HOH560 |
A | GLY13 |
A | HOH565 |
A | HOH576 |
A | HOH594 |
A | HOH595 |
A | HOH600 |
B | SER82 |
B | HOH538 |
A | GLN14 |
A | THR15 |
A | ARG35 |
A | ARG39 |
A | ASP54 |
A | VAL55 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue A80 A 402 |
Chain | Residue |
A | MET1 |
A | LEU81 |
A | PHE113 |
A | TRP116 |
A | PRO152 |
A | HIS153 |
A | ARG170 |
A | ARG174 |
A | TYR200 |
A | NAP401 |
A | HOH548 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 403 |
Chain | Residue |
A | SER173 |
A | ARG174 |
A | HOH509 |
A | HOH525 |
A | HOH531 |
site_id | AC4 |
Number of Residues | 26 |
Details | binding site for residue NAP B 401 |
Chain | Residue |
A | ASP36 |
A | SER38 |
A | HOH501 |
B | GLY10 |
B | THR12 |
B | GLY13 |
B | GLN14 |
B | THR15 |
B | ARG35 |
B | ARG39 |
B | ASP54 |
B | VAL55 |
B | LEU75 |
B | GLY76 |
B | ARG78 |
B | CYS109 |
B | THR110 |
B | SER111 |
B | HIS132 |
B | PRO151 |
B | PRO152 |
B | ILE154 |
B | SO4406 |
B | HOH511 |
B | HOH563 |
B | HOH572 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue SO4 B 402 |
Chain | Residue |
A | ARG140 |
A | HOH616 |
B | HIS153 |
B | GLY155 |
B | ASP156 |
B | GLN157 |
B | VAL175 |
B | HOH507 |
B | HOH546 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 403 |
Chain | Residue |
A | ALA48 |
A | HIS49 |
B | LYS137 |
B | HOH501 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 404 |
Chain | Residue |
A | HIS183 |
B | LYS4 |
B | HOH512 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 405 |
Chain | Residue |
B | ALA26 |
B | TYR28 |
B | HOH509 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 406 |
Chain | Residue |
B | HIS153 |
B | NAP401 |
B | HOH529 |
A | ARG134 |
B | ARG78 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: S-nitroso-cysteine intermediate; for S-nitroso-CoA-dependent nitrosyltransferase activity => ECO:0000269|PubMed:38056462 |
Chain | Residue | Details |
A | CYS109 | |
A | CYS188 | |
B | CYS109 | |
B | CYS188 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11224564, ECO:0000269|PubMed:29487133, ECO:0000269|PubMed:34957824, ECO:0007744|PDB:1HDO, ECO:0007744|PDB:5OOG, ECO:0007744|PDB:5OOH, ECO:0007744|PDB:7ER7 |
Chain | Residue | Details |
A | GLY10 | |
B | GLY10 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11224564, ECO:0000269|PubMed:29487133, ECO:0000269|PubMed:32246827, ECO:0000269|PubMed:34957824, ECO:0007744|PDB:1HDO, ECO:0007744|PDB:1HE2, ECO:0007744|PDB:1HE3, ECO:0007744|PDB:1HE4, ECO:0007744|PDB:1HE5, ECO:0007744|PDB:5OOG, ECO:0007744|PDB:5OOH, ECO:0007744|PDB:6OPL, ECO:0007744|PDB:7ER6, ECO:0007744|PDB:7ER7, ECO:0007744|PDB:7ER8, ECO:0007744|PDB:7ER9, ECO:0007744|PDB:7ERA, ECO:0007744|PDB:7ERB, ECO:0007744|PDB:7ERC, ECO:0007744|PDB:7ERD, ECO:0007744|PDB:7ERE |
Chain | Residue | Details |
A | THR12 | |
B | THR15 | |
B | ARG35 | |
B | ASP54 | |
B | VAL55 | |
B | GLY76 | |
B | ARG78 | |
B | MET87 | |
A | THR15 | |
A | ARG35 | |
A | ASP54 | |
A | VAL55 | |
A | GLY76 | |
A | ARG78 | |
A | MET87 | |
B | THR12 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11224564, ECO:0000269|PubMed:32246827, ECO:0000269|PubMed:34957824, ECO:0007744|PDB:1HDO, ECO:0007744|PDB:1HE2, ECO:0007744|PDB:1HE3, ECO:0007744|PDB:1HE4, ECO:0007744|PDB:1HE5, ECO:0007744|PDB:5OOG, ECO:0007744|PDB:5OOH, ECO:0007744|PDB:6OPL, ECO:0007744|PDB:7ER6, ECO:0007744|PDB:7ER7, ECO:0007744|PDB:7ER8, ECO:0007744|PDB:7ER9, ECO:0007744|PDB:7ERA, ECO:0007744|PDB:7ERB, ECO:0007744|PDB:7ERC, ECO:0007744|PDB:7ERD, ECO:0007744|PDB:7ERE |
Chain | Residue | Details |
A | GLY13 | |
B | GLY13 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11224564, ECO:0000269|PubMed:29487133, ECO:0000269|PubMed:34957824, ECO:0007744|PDB:1HDO, ECO:0007744|PDB:1HE2, ECO:0007744|PDB:1HE3, ECO:0007744|PDB:1HE4, ECO:0007744|PDB:1HE5, ECO:0007744|PDB:5OOG, ECO:0007744|PDB:5OOH, ECO:0007744|PDB:7ER6, ECO:0007744|PDB:7ER7, ECO:0007744|PDB:7ER8, ECO:0007744|PDB:7ER9, ECO:0007744|PDB:7ERA, ECO:0007744|PDB:7ERB, ECO:0007744|PDB:7ERC, ECO:0007744|PDB:7ERD, ECO:0007744|PDB:7ERE |
Chain | Residue | Details |
A | GLN14 | |
A | ILE154 | |
B | GLN14 | |
B | ILE154 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:34957824, ECO:0007744|PDB:7ER6, ECO:0007744|PDB:7ER9, ECO:0007744|PDB:7ERA, ECO:0007744|PDB:7ERB, ECO:0007744|PDB:7ERD, ECO:0007744|PDB:7ERE |
Chain | Residue | Details |
A | SER38 | |
B | SER38 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29487133, ECO:0000269|PubMed:32246827, ECO:0000269|PubMed:34957824, ECO:0007744|PDB:5OOH, ECO:0007744|PDB:6OPL, ECO:0007744|PDB:7ER6, ECO:0007744|PDB:7ER7, ECO:0007744|PDB:7ER8, ECO:0007744|PDB:7ER9, ECO:0007744|PDB:7ERA, ECO:0007744|PDB:7ERB, ECO:0007744|PDB:7ERC, ECO:0007744|PDB:7ERE |
Chain | Residue | Details |
A | ARG39 | |
B | ARG39 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11224564, ECO:0000269|PubMed:32246827, ECO:0000269|PubMed:34957824, ECO:0007744|PDB:1HDO, ECO:0007744|PDB:1HE2, ECO:0007744|PDB:1HE3, ECO:0007744|PDB:1HE4, ECO:0007744|PDB:1HE5, ECO:0007744|PDB:6OPL, ECO:0007744|PDB:7ER6, ECO:0007744|PDB:7ER7, ECO:0007744|PDB:7ER8, ECO:0007744|PDB:7ER9, ECO:0007744|PDB:7ERA, ECO:0007744|PDB:7ERB, ECO:0007744|PDB:7ERC, ECO:0007744|PDB:7ERD, ECO:0007744|PDB:7ERE |
Chain | Residue | Details |
A | LEU75 | |
B | LEU75 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11224564, ECO:0000269|PubMed:29487133, ECO:0000269|PubMed:32246827, ECO:0000269|PubMed:34957824, ECO:0007744|PDB:1HDO, ECO:0007744|PDB:1HE2, ECO:0007744|PDB:1HE3, ECO:0007744|PDB:1HE4, ECO:0007744|PDB:1HE5, ECO:0007744|PDB:5OOH, ECO:0007744|PDB:6OPL, ECO:0007744|PDB:7ER6, ECO:0007744|PDB:7ER7, ECO:0007744|PDB:7ER8, ECO:0007744|PDB:7ER9, ECO:0007744|PDB:7ERA, ECO:0007744|PDB:7ERB, ECO:0007744|PDB:7ERC, ECO:0007744|PDB:7ERD, ECO:0007744|PDB:7ERE |
Chain | Residue | Details |
A | CYS109 | |
B | CYS109 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11224564, ECO:0000269|PubMed:29487133, ECO:0000269|PubMed:32246827, ECO:0000269|PubMed:34957824, ECO:0007744|PDB:1HE3, ECO:0007744|PDB:5OOG, ECO:0007744|PDB:5OOH, ECO:0007744|PDB:6OPL, ECO:0007744|PDB:7ER8, ECO:0007744|PDB:7ER9, ECO:0007744|PDB:7ERB, ECO:0007744|PDB:7ERC |
Chain | Residue | Details |
A | HIS132 | |
B | HIS132 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:32246827, ECO:0000269|PubMed:34957824, ECO:0007744|PDB:6OPL, ECO:0007744|PDB:7ERB, ECO:0007744|PDB:7ERD |
Chain | Residue | Details |
A | HIS153 | |
B | HIS153 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER42 | |
B | SER42 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER82 | |
B | SER82 |