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1O96

Structure of electron transferring flavoprotein for Methylophilus methylotrophus.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005829cellular_componentcytosol
A0009055molecular_functionelectron transfer activity
A0009063biological_processamino acid catabolic process
A0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
B0009055molecular_functionelectron transfer activity
B0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
B0050660molecular_functionflavin adenine dinucleotide binding
C0000166molecular_functionnucleotide binding
C0005829cellular_componentcytosol
C0009055molecular_functionelectron transfer activity
C0009063biological_processamino acid catabolic process
C0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
D0009055molecular_functionelectron transfer activity
D0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
D0050660molecular_functionflavin adenine dinucleotide binding
E0000166molecular_functionnucleotide binding
E0005829cellular_componentcytosol
E0009055molecular_functionelectron transfer activity
E0009063biological_processamino acid catabolic process
E0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
F0009055molecular_functionelectron transfer activity
F0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
F0050660molecular_functionflavin adenine dinucleotide binding
Q0000166molecular_functionnucleotide binding
Q0005829cellular_componentcytosol
Q0009055molecular_functionelectron transfer activity
Q0009063biological_processamino acid catabolic process
Q0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
Z0009055molecular_functionelectron transfer activity
Z0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
Z0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AMP A1263
ChainResidue
AALA6
ASER122
ATYR127
AALA128
ASER129
ATHR130
AVAL7
ALYS8
AASN36
AASP39
AVAL64
AALA118
AGLY119
AGLN121

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FAD B1319
ChainResidue
ATRP38
AGLN121
AGLN183
BGLY209
BARG210
BGLY211
BSER235
BARG236
BPRO237
BGLN249
BVAL250
BGLY251
BGLN252
BSER253
BGLY267
BSER269
BSER271
BGLN273
BHIS274
BASN288
BTHR289
BASP290
BALA305
BASP306
BILE307

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AMP C1262
ChainResidue
CALA6
CVAL7
CLYS8
CASN36
CASP39
CVAL62
CSER63
CVAL64
CVAL100
CLEU104
CALA118
CGLY119
CGLN121
CSER122
CTYR127
CALA128
CSER129
CTHR130

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FAD D1319
ChainResidue
CGLN121
CGLN183
DGLY209
DARG210
DSER235
DARG236
DPRO237
DGLN249
DVAL250
DGLY251
DGLN252
DSER253
DGLY254
DGLY267
DILE268
DSER269
DSER271
DGLN273
DHIS274
DASN288
DTHR289
DASP290
DALA305
DASP306
DILE307

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AMP E1262
ChainResidue
EALA6
EVAL7
ELYS8
EASN36
EASP39
EVAL62
ESER63
EVAL64
EVAL100
EALA118
EGLY119
EGLN121
ESER122
ETYR127
EALA128
ESER129
ETHR130

site_idAC6
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FAD F1319
ChainResidue
EGLN121
EGLN183
FGLY209
FARG210
FGLY211
FSER235
FARG236
FPRO237
FGLN249
FVAL250
FGLY251
FGLN252
FSER253
FGLY254
FGLY267
FSER269
FSER271
FGLN273
FHIS274
FASN288
FTHR289
FASP290
FALA305
FASP306
FILE307

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AMP Q1262
ChainResidue
QALA6
QVAL7
QLYS8
QASN36
QASP39
QVAL62
QSER63
QVAL64
QVAL100
QALA118
QGLY119
QGLN121
QSER122
QTYR127
QALA128
QSER129
QTHR130

site_idAC8
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD Z1319
ChainResidue
QGLN183
QLEU184
ZGLY209
ZARG210
ZSER235
ZARG236
ZPRO237
ZGLN249
ZVAL250
ZGLY251
ZGLN252
ZSER253
ZGLY254
ZGLY267
ZSER269
ZSER271
ZGLN273
ZHIS274
ZASN288
ZTHR289
ZASP290
ZALA305
ZILE307

Functional Information from PROSITE/UniProt
site_idPS01065
Number of Residues22
DetailsETF_BETA Electron transfer flavoprotein beta-subunit signature. IrRelEGGmlQeVeincPaVLT
ChainResidueDetails
AILE160-THR181

site_idPS00696
Number of Residues27
DetailsETF_ALPHA Electron transfer flavoprotein alpha-subunit signature. LYVAmGISGsIQHmaGmkhvptIiAVN
ChainResidueDetails
BLEU262-ASN288

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:12567183, ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR, ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU
ChainResidueDetails
BGLY211
DILE268
DTHR289
DILE307
FGLY211
FARG236
FVAL250
FILE268
FTHR289
FILE307
ZGLY211
BARG236
ZARG236
ZVAL250
ZILE268
ZTHR289
ZILE307
BVAL250
BILE268
BTHR289
BILE307
DGLY211
DARG236
DVAL250

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:1O94, ECO:0007744|PDB:1O95, ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR, ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU
ChainResidueDetails
AVAL64
CVAL64
EVAL64
QVAL64

219140

PDB entries from 2024-05-01

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