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5YJY

Structure of the Ndi1 protein from Saccharomyces cerevisiae in complex with AC0-12.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003954molecular_functionNADH dehydrogenase activity
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0006116biological_processNADH oxidation
A0006120biological_processmitochondrial electron transport, NADH to ubiquinone
A0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0043065biological_processpositive regulation of apoptotic process
A0050136molecular_functionNADH:ubiquinone reductase (non-electrogenic) activity
A0055085biological_processtransmembrane transport
B0003954molecular_functionNADH dehydrogenase activity
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005759cellular_componentmitochondrial matrix
B0006116biological_processNADH oxidation
B0006120biological_processmitochondrial electron transport, NADH to ubiquinone
B0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
B0043065biological_processpositive regulation of apoptotic process
B0050136molecular_functionNADH:ubiquinone reductase (non-electrogenic) activity
B0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues32
Detailsbinding site for residue FAD A 601
ChainResidue
AGLY60
ATHR91
APRO92
ALEU94
AALA129
AALA175
AVAL176
AGLY177
ALEU195
ALYS196
ATHR239
ASER61
AARG344
AGLY382
AASP383
APRO391
ATHR392
AALA393
ATYR482
AMG602
AMG603
AMG604
AGLY62
AMG605
A8WF606
AMES607
ATRP63
AGLY64
AILE82
ASER83
APRO84
AARG85

site_idAC2
Number of Residues7
Detailsbinding site for residue MG A 602
ChainResidue
AALA175
AGLY177
AILE381
AGLY382
AASP383
AASN384
AFAD601

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 603
ChainResidue
AGLY62
AGLY64
AALA65
AALA175
AFAD601

site_idAC4
Number of Residues4
Detailsbinding site for residue MG A 604
ChainResidue
AGLY62
AARG85
ALEU89
AFAD601

site_idAC5
Number of Residues5
Detailsbinding site for residue MG A 605
ChainResidue
AGLY177
AALA178
ALYS196
AASP383
AFAD601

site_idAC6
Number of Residues3
Detailsbinding site for residue 8WF A 606
ChainResidue
AGLN394
AMET485
AFAD601

site_idAC7
Number of Residues7
Detailsbinding site for residue MES A 607
ChainResidue
APRO180
ALEU195
APRO238
ATHR239
ATHR339
AGLY340
AFAD601

site_idAC8
Number of Residues34
Detailsbinding site for residue FAD B 601
ChainResidue
BGLY60
BSER61
BGLY62
BTRP63
BGLY64
BILE82
BSER83
BPRO84
BARG85
BTHR91
BPRO92
BLEU94
BPRO95
BGLU128
BALA129
BALA175
BVAL176
BGLY177
BLEU195
BTHR239
BARG344
BGLY382
BASP383
BPRO391
BTHR392
BALA393
BGLN394
BTYR482
BMG602
BMG603
BMG604
BMG605
B8WF606
BMES607

site_idAC9
Number of Residues7
Detailsbinding site for residue MG B 602
ChainResidue
BGLY177
BILE381
BASP383
BASN384
BFAD601
BALA175
BVAL176

site_idAD1
Number of Residues5
Detailsbinding site for residue MG B 603
ChainResidue
BGLY62
BGLY64
BALA65
BALA175
BFAD601

site_idAD2
Number of Residues6
Detailsbinding site for residue MG B 604
ChainResidue
BGLY62
BTRP63
BARG85
BLEU89
BTHR91
BFAD601

site_idAD3
Number of Residues5
Detailsbinding site for residue MG B 605
ChainResidue
BGLY177
BALA178
BLYS196
BASP383
BFAD601

site_idAD4
Number of Residues4
Detailsbinding site for residue 8WF B 606
ChainResidue
BGLN394
BLEU444
BMET485
BFAD601

site_idAD5
Number of Residues7
Detailsbinding site for residue MES B 607
ChainResidue
BLEU195
BGLY237
BPRO238
BTHR239
BGLY340
BASN341
BFAD601

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BLEU229
BASN55

219869

PDB entries from 2024-05-15

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