1LC0
Structure of Biliverdin Reductase and the Enzyme-NADH Complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000165 | biological_process | MAPK cascade |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000978 | molecular_function | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| A | 0004074 | molecular_function | biliverdin reductase [NAD(P)H] activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005977 | biological_process | glycogen metabolic process |
| A | 0006309 | biological_process | apoptotic DNA fragmentation |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006641 | biological_process | triglyceride metabolic process |
| A | 0006935 | biological_process | chemotaxis |
| A | 0006954 | biological_process | inflammatory response |
| A | 0006955 | biological_process | immune response |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0007249 | biological_process | canonical NF-kappaB signal transduction |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008286 | biological_process | insulin receptor signaling pathway |
| A | 0009986 | cellular_component | cell surface |
| A | 0010467 | biological_process | gene expression |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0032094 | biological_process | response to food |
| A | 0032496 | biological_process | response to lipopolysaccharide |
| A | 0034440 | biological_process | lipid oxidation |
| A | 0038178 | biological_process | complement component C5a signaling pathway |
| A | 0042167 | biological_process | heme catabolic process |
| A | 0042440 | biological_process | pigment metabolic process |
| A | 0042593 | biological_process | glucose homeostasis |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0043491 | biological_process | phosphatidylinositol 3-kinase/protein kinase B signal transduction |
| A | 0043583 | biological_process | ear development |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106276 | molecular_function | biliberdin reductase (NADH) activity |
| A | 0106277 | molecular_function | biliverdin reductase (NADPH) activity |
| A | 0160025 | biological_process | sensory perception of itch |
| A | 1901142 | biological_process | insulin metabolic process |
| A | 1903409 | biological_process | reactive oxygen species biosynthetic process |
| A | 1905237 | biological_process | response to cyclosporin A |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 601 |
| Chain | Residue |
| A | VAL16 |
| A | SER43 |
| A | ARG44 |
| A | ARG45 |
| A | LYS209 |
| A | HOH1031 |
| A | HOH1070 |
| A | HOH1171 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 602 |
| Chain | Residue |
| A | PHE103 |
| A | ALA104 |
| A | SER285 |
| A | LYS289 |
| A | HOH1121 |
| A | HOH1253 |
| A | HOH1293 |
| A | HOH1299 |
| A | SER102 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 603 |
| Chain | Residue |
| A | GLY17 |
| A | ARG18 |
| A | HOH1061 |
| A | HOH1064 |
| A | HOH1322 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12079357","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LC3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P53004","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P53004","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P53004","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P53004","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
