Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2A1U

Crystal structure of the human ETF E165betaA mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0009055molecular_functionelectron transfer activity
A0009063biological_processamino acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0022904biological_processrespiratory electron transport chain
A0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
A0045251cellular_componentelectron transfer flavoprotein complex
A0050660molecular_functionflavin adenine dinucleotide binding
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0009055molecular_functionelectron transfer activity
B0009063biological_processamino acid catabolic process
B0022904biological_processrespiratory electron transport chain
B0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
B0045251cellular_componentelectron transfer flavoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE FAD A 599
ChainResidue
AASP208
AGLY264
AGLN265
ATHR266
AGLY267
AGLY279
AILE280
ASER281
AGLN285
AHIS286
AASN300
AGLY222
ALYS301
AASP302
AALA317
AASP318
ALEU319
AHOH619
AHOH634
BLEU185
AARG223
AGLY224
ASER248
AARG249
AALA250
AGLN262
AVAL263

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AMP B 600
ChainResidue
BALA9
BVAL10
BLYS11
BASN39
BCYS42
BCYS66
BVAL104
BLEU122
BGLY123
BGLN125
BALA126
BASP129
BCYS131
BASN132
BGLN133
BTHR134
BHOH617

Functional Information from PROSITE/UniProt
site_idPS01065
Number of Residues21
DetailsETF_BETA Electron transfer flavoprotein beta-subunit signature. VeRaiDGGl.EtLrlklPaVVT
ChainResidueDetails
BVAL162-THR182

site_idPS00696
Number of Residues27
DetailsETF_ALPHA Electron transfer flavoprotein alpha-subunit signature. LYIAvGISGaIQHlaGmkdsktIvAIN
ChainResidueDetails
ALEU274-ASN300

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055, ECO:0007744|PDB:1EFV, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T
ChainResidueDetails
BGLY123
AASN300
AASP318
BALA9
BASN39
BCYS66

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:25944712
ChainResidueDetails
ALYS158
ALYS203
ALYS226
ALYS232
BALA2
ALYS69
ALYS85

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
BLYS200
ALYS75
ALYS101
ALYS139
ALYS164

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by ETFBKMT => ECO:0000269|PubMed:25023281, ECO:0000269|PubMed:25416781
ChainResidueDetails
BLYS203

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DCW4
ChainResidueDetails
BLYS248
BLYS210

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER226
ALYS301
BSER223

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCW4
ChainResidueDetails
BLYS238

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon