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3RKO

Crystal structure of the membrane domain of respiratory complex I from E. coli at 3.0 angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
A0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
B0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
B0042773biological_processATP synthesis coupled electron transport
C0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
C0042773biological_processATP synthesis coupled electron transport
D0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
D0042773biological_processATP synthesis coupled electron transport
E0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
E0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
F0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
G0005886cellular_componentplasma membrane
G0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
G0030964cellular_componentNADH dehydrogenase complex
G0042773biological_processATP synthesis coupled electron transport
G0048038molecular_functionquinone binding
G0050136molecular_functionNADH:ubiquinone reductase (non-electrogenic) activity
J0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
K0005886cellular_componentplasma membrane
K0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
K0030964cellular_componentNADH dehydrogenase complex
K0042773biological_processATP synthesis coupled electron transport
K0048038molecular_functionquinone binding
K0050136molecular_functionNADH:ubiquinone reductase (non-electrogenic) activity
L0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
L0042773biological_processATP synthesis coupled electron transport
M0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
M0042773biological_processATP synthesis coupled electron transport
N0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
N0042773biological_processATP synthesis coupled electron transport
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LFA L 614
ChainResidue
LLYS169
LVAL173
LPHE549

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LFA L 615
ChainResidue
MMET398
MPRO399
MLFA512
LALA19
LARG22
LTYR119
LLEU148
MALA386
MLEU389

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LFA L 616
ChainResidue
LSER90
LPHE340
LLEU463

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CA7 M 510
ChainResidue
LMET168
LPHE549
LPHE553
LLEU554
MVAL434
MHIS441
MARG442
MPHE445
MGLY446
MLYS447

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LFA M 511
ChainResidue
MTYR221
MALA232
MVAL237
MVAL238
MLEU240
MLEU293

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LFA M 512
ChainResidue
LPHE20
LLFA615
MTRP383
MALA386
MLEU387
MPHE480

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LFA N 486
ChainResidue
NTRP408

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LFA N 487
ChainResidue
NVAL42
NILE43
NASN46
NTYR92

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LFA N 488
ChainResidue
NMET74
NLEU75
NLEU480
NALA481

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LFA N 489
ChainResidue
NTRP408

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LFA B 614
ChainResidue
BLYS169
BVAL172
BVAL173
BLEU235
BPHE549
BVAL550

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LFA B 615
ChainResidue
BALA19
BARG22
BTYR119
BLEU148
CALA386
CLEU389
CMET398
CPRO399
CLFA513

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LFA B 616
ChainResidue
BSER90
BPHE340
BLEU463

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CA7 C 510
ChainResidue
BMET168
BPHE553
BLEU554
CVAL434
CHIS441
CARG442
CPHE445
CGLY446
CLYS447

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LFA C 511
ChainResidue
CTYR221
CALA232
CVAL237
CVAL238
CLEU240
CLEU293

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE LFA C 512
ChainResidue
CLEU223
DTRP408

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LFA C 513
ChainResidue
BPHE20
BLFA615
CTRP383
CALA386
CLEU387
CPHE480

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LFA D 486
ChainResidue
DVAL42
DASN46
DCYS88
DTHR89
DTYR92

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LFA D 487
ChainResidue
DMET74
DLEU75
DALA481

site_idCC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LFA D 488
ChainResidue
DTRP408

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues120
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_01456
ChainResidueDetails
KLEU4-ILE24
KLEU28-VAL48
KVAL60-LEU80
GLEU4-ILE24
GLEU28-VAL48
GVAL60-LEU80

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PDB entries from 2024-08-28

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