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3EYW

Crystal structure of the C-terminal domain of E. coli KefC in complex with KefF

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 A2400
ChainResidue
AHIS1008
ATYR1068
ATHR1105
ATHR1106
AGLY1107
AGLY1108
APHE1113
ATHR1148
ASER1014
AHIS1015
AALA1016
AASN1017
APRO1064
AMET1065
AGLN1066
ATRP1067

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAD A2401
ChainResidue
AHOH127
AHOH161
AGLY406
AGLY408
AARG409
APHE410
AASP429
AHIS430
AASP431
AHIS434
AGLY448
AASP449
AALA450
AILE471
AASP472
ATHR476
AARG496
AMG2403

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A2403
ChainResidue
AGLY406
AGLY408
AGLY411
AALA470
AARG496
ANAD2401

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A2402
ChainResidue
ATYR1010
APRO1011
AHIS1012
BHOH61

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B2402
ChainResidue
AHOH99
BTYR1010
BPRO1011
BHIS1012
BHIS1013

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FMN B2400
ChainResidue
BHOH97
BHOH162
BHOH191
BHIS1008
BSER1014
BHIS1015
BALA1016
BASN1017
BPRO1064
BMET1065
BGLN1066
BTRP1067
BTYR1068
BTHR1105
BTHR1106
BGLY1107
BGLY1108
BHIS1112
BPHE1113
BTHR1148

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAD B2401
ChainResidue
BHOH128
BHOH129
BGLY406
BGLY408
BARG409
BPHE410
BASP429
BHIS430
BASP431
BHIS434
BGLY448
BASP449
BALA450
BASP472
BTHR476
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

222415

PDB entries from 2024-07-10

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