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7BN7

Crystal structure of ene-reductase OYE2 from S. cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0003959molecular_functionNADPH dehydrogenase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0006915biological_processapoptotic process
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
B0003959molecular_functionNADPH dehydrogenase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0006915biological_processapoptotic process
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
C0003959molecular_functionNADPH dehydrogenase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0006915biological_processapoptotic process
C0010181molecular_functionFMN binding
C0016491molecular_functionoxidoreductase activity
D0003959molecular_functionNADPH dehydrogenase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0006915biological_processapoptotic process
D0010181molecular_functionFMN binding
D0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue FMN A 501
ChainResidue
APRO35
AGLY325
AASN326
AGLY348
AARG349
ATYR376
AGOL502
AHOH628
AHOH639
AHOH677
APRO36
ALEU37
ATHR38
AGLY73
AGLN115
AHIS192
AASN195
AARG244

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 502
ChainResidue
AHIS192
AASN195
ATYR197
APHE251
APRO296
ATYR376
AFMN501

site_idAC3
Number of Residues19
Detailsbinding site for residue FMN B 501
ChainResidue
BPRO35
BPRO36
BLEU37
BTHR38
BGLY73
BGLN115
BHIS192
BASN195
BARG244
BGLY325
BASN326
BGLY348
BARG349
BPHE375
BTYR376
BGOL502
BHOH604
BHOH623
BHOH643

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL B 502
ChainResidue
BASN195
BTYR197
BPHE251
BPRO296
BTYR376
BFMN501
BHOH643

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL B 503
ChainResidue
BSER309
BHOH614
DHOH629

site_idAC6
Number of Residues19
Detailsbinding site for residue FMN C 501
ChainResidue
CPRO35
CPRO36
CLEU37
CTHR38
CGLY73
CGLN115
CHIS192
CASN195
CARG244
CGLY325
CASN326
CGLY348
CARG349
CPHE375
CTYR376
CGOL502
CHOH607
CHOH630
CHOH638

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL C 502
ChainResidue
CTRP117
CHIS192
CASN195
CTYR197
CPHE251
CPRO296
CFMN501

site_idAC8
Number of Residues18
Detailsbinding site for residue FMN D 501
ChainResidue
DPRO35
DPRO36
DLEU37
DTHR38
DGLY73
DGLN115
DHIS192
DASN195
DARG244
DGLY325
DASN326
DGLY348
DARG349
DPHE375
DGOL502
DHOH623
DHOH630
DHOH659

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL D 502
ChainResidue
DASN195
DTYR197
DPHE251
DPRO296
DTYR376
DFMN501
DHIS192

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q02899
ChainResidueDetails
ATYR197
BTYR197
CTYR197
DTYR197

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q02899
ChainResidueDetails
ATHR38
BHIS192
BASN195
BARG244
BARG349
BTYR376
CTHR38
CGLN115
CHIS192
CASN195
CARG244
AGLN115
CARG349
CTYR376
DTHR38
DGLN115
DHIS192
DASN195
DARG244
DARG349
DTYR376
AHIS192
AASN195
AARG244
AARG349
ATYR376
BTHR38
BGLN115

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER353
BSER353
CSER353
DSER353

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER379
BSER379
CSER379
DSER379

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PDB entries from 2024-11-06

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