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1Z6Z

Crystal Structure of Human Sepiapterin Reductase in complex with NADP+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004757molecular_functionsepiapterin reductase (NADP+) activity
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006729biological_processtetrahydrobiopterin biosynthetic process
A0006809biological_processnitric oxide biosynthetic process
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0016491molecular_functionoxidoreductase activity
A0050661molecular_functionNADP binding
A0070062cellular_componentextracellular exosome
B0004757molecular_functionsepiapterin reductase (NADP+) activity
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006729biological_processtetrahydrobiopterin biosynthetic process
B0006809biological_processnitric oxide biosynthetic process
B0008106molecular_functionalcohol dehydrogenase (NADP+) activity
B0016491molecular_functionoxidoreductase activity
B0050661molecular_functionNADP binding
B0070062cellular_componentextracellular exosome
C0004757molecular_functionsepiapterin reductase (NADP+) activity
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0006729biological_processtetrahydrobiopterin biosynthetic process
C0006809biological_processnitric oxide biosynthetic process
C0008106molecular_functionalcohol dehydrogenase (NADP+) activity
C0016491molecular_functionoxidoreductase activity
C0050661molecular_functionNADP binding
C0070062cellular_componentextracellular exosome
D0004757molecular_functionsepiapterin reductase (NADP+) activity
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005829cellular_componentcytosol
D0006729biological_processtetrahydrobiopterin biosynthetic process
D0006809biological_processnitric oxide biosynthetic process
D0008106molecular_functionalcohol dehydrogenase (NADP+) activity
D0016491molecular_functionoxidoreductase activity
D0050661molecular_functionNADP binding
D0070062cellular_componentextracellular exosome
E0004757molecular_functionsepiapterin reductase (NADP+) activity
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005739cellular_componentmitochondrion
E0005829cellular_componentcytosol
E0006729biological_processtetrahydrobiopterin biosynthetic process
E0006809biological_processnitric oxide biosynthetic process
E0008106molecular_functionalcohol dehydrogenase (NADP+) activity
E0016491molecular_functionoxidoreductase activity
E0050661molecular_functionNADP binding
E0070062cellular_componentextracellular exosome
F0004757molecular_functionsepiapterin reductase (NADP+) activity
F0005654cellular_componentnucleoplasm
F0005737cellular_componentcytoplasm
F0005739cellular_componentmitochondrion
F0005829cellular_componentcytosol
F0006729biological_processtetrahydrobiopterin biosynthetic process
F0006809biological_processnitric oxide biosynthetic process
F0008106molecular_functionalcohol dehydrogenase (NADP+) activity
F0016491molecular_functionoxidoreductase activity
F0050661molecular_functionNADP binding
F0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ALYS87
AGLY88
ALEU89
CARG45

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 401
ChainResidue
AARG39

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL C 402
ChainResidue
CARG39

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL D 403
ChainResidue
DARG39

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL C 405
ChainResidue
CGLY88

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 406
ChainResidue
CTYR167
CNAP803
BTYR-4

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 407
ChainResidue
ASER154
ATYR167
ANAP801

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 408
ChainResidue
BSER154
BTYR167
BNAP802

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL D 409
ChainResidue
DSER154
DTYR167
DNAP804

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL E 410
ChainResidue
ESER154
ETYR167
ENAP805

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL F 411
ChainResidue
FSER154
FTYR167
FNAP806

site_idBC3
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAP A 801
ChainResidue
AGLY11
ASER13
AARG14
AGLY15
APHE16
AALA38
AARG39
AASN40
AALA65
AASP66
ALEU67
AASN97
ALEU123
AILE152
ASER153
ATYR167
ALYS171
APRO195
AGLY196
APRO197
ALEU198
ATHR200
AMET202
AGLN203
ACL407
AHOH802
AHOH808
AHOH831
AHOH843
AHOH851
AHOH856

site_idBC4
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAP B 802
ChainResidue
BGLY11
BSER13
BARG14
BGLY15
BPHE16
BARG39
BASN40
BALA65
BASP66
BLEU67
BASN97
BALA98
BLEU123
BILE152
BSER153
BTYR167
BLYS171
BPRO195
BGLY196
BPRO197
BLEU198
BTHR200
BMET202
BGLN203
BCL408
BHOH826
BHOH829

site_idBC5
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAP C 803
ChainResidue
CTYR167
CLYS171
CPRO195
CGLY196
CPRO197
CLEU198
CTHR200
CMET202
CGLN203
CCL406
CHOH808
CHOH836
CHOH837
CHOH857
CHOH863
CGLY11
CSER13
CARG14
CGLY15
CPHE16
CARG39
CASN40
CALA65
CASP66
CLEU67
CASN97
CALA98
CLEU123
CILE152
CSER153

site_idBC6
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAP D 804
ChainResidue
DGLY11
DSER13
DARG14
DGLY15
DPHE16
DALA38
DARG39
DASN40
DALA65
DASP66
DLEU67
DASN97
DALA98
DLEU123
DILE152
DSER153
DTYR167
DLYS171
DPRO195
DGLY196
DPRO197
DLEU198
DTHR200
DMET202
DGLN203
DCL409
DHOH808
DHOH811
DHOH817
DHOH837

site_idBC7
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAP E 805
ChainResidue
EGLY11
ESER13
EARG14
EGLY15
EPHE16
EARG39
EASN40
EALA65
EASP66
ELEU67
EASN97
ELEU123
EILE152
ESER153
ETYR167
ELYS171
EPRO195
EGLY196
EPRO197
ELEU198
ETHR200
EMET202
EGLN203
ECL410

site_idBC8
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAP F 806
ChainResidue
FGLY11
FSER13
FARG14
FGLY15
FPHE16
FARG39
FASN40
FALA65
FASP66
FLEU67
FASN97
FLEU123
FILE152
FSER153
FTYR167
FLYS171
FPRO195
FGLY196
FPRO197
FLEU198
FTHR200
FMET202
FGLN203
FCL411
FHOH815

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues78
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human sepiapterin reductase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues30
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P18297","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine; by CaMK2; in vitro","evidences":[{"source":"PubMed","id":"11825621","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ASER154
ATYR167
AASN124
ALYS171

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
DTRP164
DLYS171

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ETRP164
ELYS171

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
FTRP164
FLYS171

site_idCSA13
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ATYR167
ALYS171

site_idCSA14
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BTYR167
BLYS171

site_idCSA15
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
CTYR167
CLYS171

site_idCSA16
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
DTYR167
DLYS171

site_idCSA17
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ETYR167
ELYS171

site_idCSA18
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
FTYR167
FLYS171

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BSER154
BTYR167
BASN124
BLYS171

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
CSER154
CTYR167
CASN124
CLYS171

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
DSER154
DTYR167
DASN124
DLYS171

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ESER154
ETYR167
EASN124
ELYS171

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
FSER154
FTYR167
FASN124
FLYS171

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ATRP164
ALYS171

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BTRP164
BLYS171

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
CTRP164
CLYS171

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PDB entries from 2025-10-08

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