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1GCU

CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0000166molecular_functionnucleotide binding
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
A0004074molecular_functionbiliverdin reductase [NAD(P)H] activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005977biological_processglycogen metabolic process
A0006309biological_processapoptotic DNA fragmentation
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006641biological_processtriglyceride metabolic process
A0006935biological_processchemotaxis
A0006954biological_processinflammatory response
A0006955biological_processimmune response
A0006979biological_processresponse to oxidative stress
A0007249biological_processcanonical NF-kappaB signal transduction
A0008270molecular_functionzinc ion binding
A0008286biological_processinsulin receptor signaling pathway
A0009986cellular_componentcell surface
A0010467biological_processgene expression
A0016491molecular_functionoxidoreductase activity
A0032094biological_processresponse to food
A0032496biological_processresponse to lipopolysaccharide
A0034440biological_processlipid oxidation
A0038178biological_processcomplement component C5a signaling pathway
A0042167biological_processheme catabolic process
A0042440biological_processpigment metabolic process
A0042593biological_processglucose homeostasis
A0043066biological_processnegative regulation of apoptotic process
A0043491biological_processphosphatidylinositol 3-kinase/protein kinase B signal transduction
A0043583biological_processear development
A0046872molecular_functionmetal ion binding
A0106276molecular_functionbiliberdin reductase (NADH) activity
A0106277molecular_functionbiliverdin reductase (NADPH) activity
A0160025biological_processsensory perception of itch
A1901142biological_processinsulin metabolic process
A1903409biological_processreactive oxygen species biosynthetic process
A1905237biological_processresponse to cyclosporin A
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12079357, ECO:0007744|PDB:1LC3
ChainResidueDetails
AARG18
ASER76
ATYR97
ASER167

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P53004
ChainResidueDetails
AHIS279
ACYS280
ACYS291
AHIS292

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER154

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P53004
ChainResidueDetails
ATHR173

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P53004
ChainResidueDetails
ASER177

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P53004
ChainResidueDetails
ALYS247
ALYS252

Catalytic Information from CSA
site_idCSA1
Number of Residues6
Detailsa catalytic site defined by CSA, PubMed 12079357, 20547221, 15870194
ChainResidueDetails
ATYR97
ASER170
AARG171
AGLU96
AGLU123
AGLU126

site_idMCSA1
Number of Residues6
DetailsM-CSA 566
ChainResidueDetails
AGLU96electrostatic stabiliser
ATYR97electrostatic stabiliser, proton acceptor, proton donor
AGLU123electrostatic stabiliser
AGLU126electrostatic stabiliser
ASER170electrostatic stabiliser
AARG171electrostatic stabiliser

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PDB entries from 2025-06-18

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