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3L9X

KefC C-terminal domain in complex with KefF and ESG

Functional Information from GO Data
ChainGOidnamespacecontents
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006813biological_processpotassium ion transport
A0008753molecular_functionNADPH dehydrogenase (quinone) activity
A0009055molecular_functionelectron transfer activity
A0010181molecular_functionFMN binding
A0015079molecular_functionpotassium ion transmembrane transporter activity
A0016491molecular_functionoxidoreductase activity
A0042803molecular_functionprotein homodimerization activity
A0050136molecular_functionNADH:ubiquinone reductase (non-electrogenic) activity
A0051453biological_processregulation of intracellular pH
A0051454biological_processintracellular pH elevation
A1901381biological_processpositive regulation of potassium ion transmembrane transport
A1903103cellular_componentpotassium:proton antiporter complex
B0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006813biological_processpotassium ion transport
B0008753molecular_functionNADPH dehydrogenase (quinone) activity
B0009055molecular_functionelectron transfer activity
B0010181molecular_functionFMN binding
B0015079molecular_functionpotassium ion transmembrane transporter activity
B0016491molecular_functionoxidoreductase activity
B0042803molecular_functionprotein homodimerization activity
B0050136molecular_functionNADH:ubiquinone reductase (non-electrogenic) activity
B0051453biological_processregulation of intracellular pH
B0051454biological_processintracellular pH elevation
B1901381biological_processpositive regulation of potassium ion transmembrane transport
B1903103cellular_componentpotassium:proton antiporter complex
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FMN A 2400
ChainResidue
AHIS1008
ATYR1068
ATHR1105
ATHR1106
AGLY1107
AGLY1108
APHE1113
ATHR1148
ASER1014
AHIS1015
AALA1016
AASN1017
APRO1064
AMET1065
AGLN1066
ATRP1067

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 2402
ChainResidue
ATYR1010
APRO1011
AHIS1012

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ESG B 1177
ChainResidue
AHOH191
AARG409
AGLN412
AILE413
AARG416
ATHR437
BHOH218
BHOH219
BHOH261
BARG498
BASP499
BVAL500
BARG516

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1190
ChainResidue
AHOH59
AHOH278
AGLY408
AARG409
APHE410
AASP472
AARG496

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 2402
ChainResidue
AHOH50
BHOH274
BTYR1010
BPRO1011
BHIS1012

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FMN B 2400
ChainResidue
BHOH197
BHOH273
BHIS1008
BSER1014
BHIS1015
BALA1016
BASN1017
BPRO1064
BMET1065
BGLN1066
BTRP1067
BTYR1068
BTHR1105
BTHR1106
BGLY1107
BGLY1108
BHIS1112
BPHE1113
BTHR1148
BPHE1149

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE L9X B 1178
ChainResidue
AHOH191
AARG409
AGLN412
AILE413
AARG416
BHOH218
BHOH219
BHOH261
BARG498
BASP499
BVAL500
BARG516
BMET558

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1180
ChainResidue
BGLY408
BARG409
BPHE410
BASP472
BARG496

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:19523906
ChainResidueDetails
AGLY408
BASP449
BASP472
BARG496
AASP429
AHIS434
AASP449
AASP472
AARG496
BGLY408
BASP429
BHIS434

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLN412
BGLN412

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: in other chain
ChainResidueDetails
AARG498
AARG516
BARG498
BARG516

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01414, ECO:0000269|PubMed:19523906, ECO:0000269|PubMed:21041667
ChainResidueDetails
AHIS1008
ASER1014
AMET1065
ATHR1105
BHIS1008
BSER1014
BMET1065
BTHR1105

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PDB entries from 2024-05-01

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