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2BPO

Crystal structure of the yeast CPR triple mutant: D74G, Y75F, K78A.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003958molecular_functionNADPH-hemoprotein reductase activity
A0003959molecular_functionNADPH dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006696biological_processergosterol biosynthetic process
A0009055molecular_functionelectron transfer activity
A0010181molecular_functionFMN binding
A0016126biological_processsterol biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
B0003958molecular_functionNADPH-hemoprotein reductase activity
B0003959molecular_functionNADPH dehydrogenase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006696biological_processergosterol biosynthetic process
B0009055molecular_functionelectron transfer activity
B0010181molecular_functionFMN binding
B0016126biological_processsterol biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 760
ChainResidue
ASER282
AASP284
AARG285
AASN582

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 761
ChainResidue
AASP626
BPRO337

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 B 762
ChainResidue
BARG553

site_idAC4
Number of Residues28
DetailsBINDING SITE FOR RESIDUE FAD A 750
ChainResidue
APRO365
ATYR405
APHE406
AASN407
AARG439
ATYR440
ATYR441
ASER442
ATHR457
ASER458
AILE459
AGLU461
APHE463
AVAL474
AVAL475
AGLY476
AVAL477
ATHR478
ATHR479
ATRP691
AFMN751
ANAP753
AHOH2073
AHOH2075
AHOH2123
AHOH2124
AHIS306
AGLY364

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN A 751
ChainResidue
ASER67
AGLN68
ATHR69
AGLY70
ATHR71
AALA72
ASER116
ATHR117
ATYR118
AGLY119
ALEU152
AGLY153
AASN154
ATYR157
AGLU158
APHE159
APHE160
AASN161
AASP187
AVAL690
AFAD750
AHOH2126
AHOH2127

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAP A 753
ChainResidue
AARG285
AILE459
AGLU461
APRO541
AGLY542
ATHR543
ASER580
AARG581
ASER610
AARG611
ALYS617
ATYR619
AGLN621
AASP646
AALA647
ALYS648
AGLY649
AMET650
AFAD750
AHOH2096
AHOH2101
AHOH2113

site_idAC7
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD B 750
ChainResidue
BTHR479
BARG522
BTRP691
BHOH2038
BHIS306
BGLY364
BPRO365
BTYR405
BPHE406
BASN407
BARG439
BTYR440
BTYR441
BSER442
BTHR457
BSER458
BILE459
BGLU461
BVAL474
BVAL475
BGLY476
BVAL477
BTHR478

site_idAC8
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN B 751
ChainResidue
BSER67
BGLN68
BTHR69
BGLY70
BTHR71
BALA72
BSER116
BTHR117
BTYR118
BGLY119
BLEU152
BGLY153
BASN154
BTYR157
BPHE159
BPHE160
BASN161
BASP187
BVAL690

site_idAC9
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAP B 753
ChainResidue
BARG285
BILE459
BGLU461
BGLY542
BTHR543
BSER580
BARG581
BSER610
BARG611
BLYS617
BTYR619
BGLN621
BASP646
BALA647
BLYS648
BGLY649
BMET650
BTRP691
BHOH2057
BHOH2058

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1332
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
APRO25-TRP691
BPRO25-TRP691

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:16407065, ECO:0000269|PubMed:19483672
ChainResidueDetails
AGLN68
ATHR117
AGLY153
BGLN68
BTHR117
BGLY153

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16407065
ChainResidueDetails
APHE79
AALA647
BPHE79
BALA647

site_idSWS_FT_FI4
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:16407065
ChainResidueDetails
AGLY188
BGLY188
BASN286
BTYR440
BSER458
BVAL477
BGLY544
BARG611
BVAL618
BTRP691
AASN286
ATYR440
ASER458
AVAL477
AGLY544
AARG611
AVAL618
ATRP691

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ASER667
BSER667

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndh
ChainResidueDetails
ASER444

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndh
ChainResidueDetails
BSER444

223166

PDB entries from 2024-07-31

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