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4CF6

Crystal structure of the complex of the P187S variant of human NAD(P) H:quinone oxidoreductase with Cibacron blue at 2.7 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0003723molecular_functionRNA binding
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0004128molecular_functioncytochrome-b5 reductase activity, acting on NAD(P)H
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006743biological_processubiquinone metabolic process
A0006805biological_processxenobiotic metabolic process
A0006809biological_processnitric oxide biosynthetic process
A0006979biological_processresponse to oxidative stress
A0007271biological_processsynaptic transmission, cholinergic
A0008753molecular_functionNADPH dehydrogenase (quinone) activity
A0009636biological_processresponse to toxic substance
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0030163biological_processprotein catabolic process
A0032496biological_processresponse to lipopolysaccharide
A0034599biological_processcellular response to oxidative stress
A0042177biological_processnegative regulation of protein catabolic process
A0042360biological_processvitamin E metabolic process
A0042373biological_processvitamin K metabolic process
A0042802molecular_functionidentical protein binding
A0045087biological_processinnate immune response
A0045202cellular_componentsynapse
A0045454biological_processcell redox homeostasis
A0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
A0061771biological_processresponse to caloric restriction
A0110076biological_processnegative regulation of ferroptosis
B0000209biological_processprotein polyubiquitination
B0003723molecular_functionRNA binding
B0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
B0004128molecular_functioncytochrome-b5 reductase activity, acting on NAD(P)H
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006743biological_processubiquinone metabolic process
B0006805biological_processxenobiotic metabolic process
B0006809biological_processnitric oxide biosynthetic process
B0006979biological_processresponse to oxidative stress
B0007271biological_processsynaptic transmission, cholinergic
B0008753molecular_functionNADPH dehydrogenase (quinone) activity
B0009636biological_processresponse to toxic substance
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0030163biological_processprotein catabolic process
B0032496biological_processresponse to lipopolysaccharide
B0034599biological_processcellular response to oxidative stress
B0042177biological_processnegative regulation of protein catabolic process
B0042360biological_processvitamin E metabolic process
B0042373biological_processvitamin K metabolic process
B0042802molecular_functionidentical protein binding
B0045087biological_processinnate immune response
B0045202cellular_componentsynapse
B0045454biological_processcell redox homeostasis
B0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
B0061771biological_processresponse to caloric restriction
B0110076biological_processnegative regulation of ferroptosis
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD A 1274
ChainResidue
AHIS12
ATRP106
APHE107
ATHR148
ATHR149
AGLY150
AGLY151
ATYR156
AILE193
AARG201
ACBD1275
ATHR16
BGLN67
BTYR68
BPRO69
BGLU118
ASER17
APHE18
AASN19
AALA21
APRO103
ALEU104
AGLN105

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FAD B 1275
ChainResidue
AGLN67
ATYR68
APRO69
AHOH2002
BHIS12
BSER17
BPHE18
BASN19
BALA21
BPRO103
BLEU104
BGLN105
BTRP106
BPHE107
BTHR148
BTHR149
BGLY150
BGLY151
BTYR156
BILE193
BARG201
BCBD1276

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE CBD A 1275
ChainResidue
AGLY150
AGLY151
AMET155
ASER192
AGLY194
AHIS195
APHE233
AGLN234
AFAD1274
BPRO69
BTYR127
BTYR129
BPHE179
BHIS195
BPHE233
BCBD1276

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE CBD B 1276
ChainResidue
APRO69
ATYR129
APHE179
AHIS195
ATHR196
APRO197
APHE233
AGLY236
APHE237
ACBD1275
BGLY150
BSER152
BSER154
BMET155
BHIS162
BSER192
BHIS195
BGLN234
BFAD1275

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
ChainResidueDetails
AHIS12
BGLN67
BLEU104
BTHR148
BTYR156
BARG201
APHE18
AGLN67
ALEU104
ATHR148
ATYR156
AARG201
BHIS12
BPHE18

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AALA126
BALA126

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER82
BSER82

site_idSWS_FT_FI4
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS250
ALYS251
BLYS250
BLYS251

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 3
ChainResidueDetails
AGLY150electrostatic stabiliser, hydrogen bond donor
ATYR156electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AHIS162hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

site_idMCSA2
Number of Residues3
DetailsM-CSA 3
ChainResidueDetails
BGLY150electrostatic stabiliser, hydrogen bond donor
BTYR156electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
BHIS162hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

237735

PDB entries from 2025-06-18

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