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7ER8

Crystal structure of human Biliverdin IX-beta reductase B with Sulfasalazine (SAS)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004074molecular_functionbiliverdin reductase [NAD(P)+] activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008752molecular_functionFMN reductase (NAD(P)H) activity
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0030219biological_processmegakaryocyte differentiation
A0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
A0042167biological_processheme catabolic process
A0042602molecular_functionriboflavin reductase (NADPH) activity
A0043231cellular_componentintracellular membrane-bounded organelle
A0046627biological_processnegative regulation of insulin receptor signaling pathway
A0052873molecular_functionFMN reductase (NADPH) activity
A0052874molecular_functionFMN reductase (NADH) activity
A0070062cellular_componentextracellular exosome
A0106276molecular_functionbiliberdin reductase (NAD+) activity
A0106277molecular_functionbiliverdin reductase (NADP+) activity
B0004074molecular_functionbiliverdin reductase [NAD(P)+] activity
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008752molecular_functionFMN reductase (NAD(P)H) activity
B0016491molecular_functionoxidoreductase activity
B0016740molecular_functiontransferase activity
B0030219biological_processmegakaryocyte differentiation
B0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
B0042167biological_processheme catabolic process
B0042602molecular_functionriboflavin reductase (NADPH) activity
B0043231cellular_componentintracellular membrane-bounded organelle
B0046627biological_processnegative regulation of insulin receptor signaling pathway
B0052873molecular_functionFMN reductase (NADPH) activity
B0052874molecular_functionFMN reductase (NADH) activity
B0070062cellular_componentextracellular exosome
B0106276molecular_functionbiliberdin reductase (NAD+) activity
B0106277molecular_functionbiliverdin reductase (NADP+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues39
Detailsbinding site for residue NAP A 401
ChainResidue
AGLY10
ALEU74
ALEU75
AGLY76
ATHR77
AARG78
AVAL86
AMET87
ACYS109
ATHR110
ASER111
ATHR12
AHIS132
APRO151
APRO152
AHIS153
AILE154
ASAS402
AHOH517
AHOH536
AHOH541
AHOH548
AGLY13
AHOH570
AHOH588
AHOH589
AHOH596
AHOH603
AHOH635
AHOH655
AHOH661
BSER82
BHOH532
AGLN14
ATHR15
AARG35
ASER38
AASP54
AVAL55

site_idAC2
Number of Residues11
Detailsbinding site for residue SAS A 402
ChainResidue
AHIS0
APHE113
ATRP116
APRO152
AHIS153
AARG170
AGLY171
AARG174
ATYR200
ANAP401
AHOH565

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 403
ChainResidue
AHIS136
AARG140
AHOH506

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 404
ChainResidue
AHIS183
AHOH650
BLYS4

site_idAC5
Number of Residues34
Detailsbinding site for residue NAP B 401
ChainResidue
ASER37
BGLY10
BTHR12
BGLY13
BGLN14
BTHR15
BARG35
BARG39
BASP54
BVAL55
BLEU74
BLEU75
BGLY76
BARG78
BMET87
BCYS109
BTHR110
BSER111
BHIS132
BPRO151
BPRO152
BILE154
BSAS402
BHOH513
BHOH514
BHOH530
BHOH531
BHOH548
BHOH576
BHOH588
BHOH591
BHOH597
BHOH600
BHOH605

site_idAC6
Number of Residues17
Detailsbinding site for residue SAS B 402
ChainResidue
BARG124
BPRO152
BHIS153
BNAP401
BHOH503
BHOH508
BHOH515
BHOH552
AGLU89
AARG134
BTHR77
BASN79
BASP80
BLEU81
BSER111
BPHE113
BTRP116

site_idAC7
Number of Residues9
Detailsbinding site for residue SO4 B 403
ChainResidue
ALYS137
AARG140
BHIS153
BGLY155
BASP156
BGLN157
BVAL175
BHOH516
BHOH551

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 B 404
ChainResidue
BVAL3
BALA26
BTYR28
BHOH519

site_idAC9
Number of Residues5
Detailsbinding site for residue SO4 B 405
ChainResidue
BLYS178
BHIS179
BHOH534
BHOH555
BHOH621

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: S-nitroso-cysteine intermediate; for S-nitroso-CoA-dependent nitrosyltransferase activity => ECO:0000269|PubMed:38056462
ChainResidueDetails
ACYS109
ACYS188
BCYS109
BCYS188

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
AGLY10
BGLY10

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: 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
ChainResidueDetails
ATHR12
BTHR15
BARG35
BASP54
BVAL55
BGLY76
BARG78
BMET87
ATHR15
AARG35
AASP54
AVAL55
AGLY76
AARG78
AMET87
BTHR12

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
AGLY13
BGLY13

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: 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
ChainResidueDetails
AGLN14
AILE154
BGLN14
BILE154

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
ASER38
BSER38

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
AARG39
BARG39

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
ALEU75
BLEU75

site_idSWS_FT_FI9
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
ACYS109
BCYS109

site_idSWS_FT_FI10
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
AHIS132
BHIS132

site_idSWS_FT_FI11
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:32246827, ECO:0000269|PubMed:34957824, ECO:0007744|PDB:6OPL, ECO:0007744|PDB:7ERB, ECO:0007744|PDB:7ERD
ChainResidueDetails
AHIS153
BHIS153

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER42
BSER42

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER82
BSER82

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PDB entries from 2024-07-24

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