2A1U
Crystal structure of the human ETF E165betaA mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0009055 | molecular_function | electron transfer activity |
A | 0009063 | biological_process | amino acid catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0022904 | biological_process | respiratory electron transport chain |
A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
A | 0045251 | cellular_component | electron transfer flavoprotein complex |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0005515 | molecular_function | protein binding |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0009055 | molecular_function | electron transfer activity |
B | 0009063 | biological_process | amino acid catabolic process |
B | 0022904 | biological_process | respiratory electron transport chain |
B | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
B | 0045251 | cellular_component | electron transfer flavoprotein complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD A 599 |
Chain | Residue |
A | ASP208 |
A | GLY264 |
A | GLN265 |
A | THR266 |
A | GLY267 |
A | GLY279 |
A | ILE280 |
A | SER281 |
A | GLN285 |
A | HIS286 |
A | ASN300 |
A | GLY222 |
A | LYS301 |
A | ASP302 |
A | ALA317 |
A | ASP318 |
A | LEU319 |
A | HOH619 |
A | HOH634 |
B | LEU185 |
A | ARG223 |
A | GLY224 |
A | SER248 |
A | ARG249 |
A | ALA250 |
A | GLN262 |
A | VAL263 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE AMP B 600 |
Chain | Residue |
B | ALA9 |
B | VAL10 |
B | LYS11 |
B | ASN39 |
B | CYS42 |
B | CYS66 |
B | VAL104 |
B | LEU122 |
B | GLY123 |
B | GLN125 |
B | ALA126 |
B | ASP129 |
B | CYS131 |
B | ASN132 |
B | GLN133 |
B | THR134 |
B | HOH617 |
Functional Information from PROSITE/UniProt
site_id | PS00696 |
Number of Residues | 27 |
Details | ETF_ALPHA Electron transfer flavoprotein alpha-subunit signature. LYIAvGISGaIQHlaGmkdsktIvAIN |
Chain | Residue | Details |
A | LEU274-ASN300 |
site_id | PS01065 |
Number of Residues | 21 |
Details | ETF_BETA Electron transfer flavoprotein beta-subunit signature. VeRaiDGGl.EtLrlklPaVVT |
Chain | Residue | Details |
B | VAL162-THR182 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: 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 |
Chain | Residue | Details |
B | ALA9 | |
B | ASN39 | |
B | CYS66 | |
B | GLY123 | |
A | ASN300 | |
A | ASP318 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:25944712 |
Chain | Residue | Details |
B | ALA2 | |
A | LYS69 | |
A | LYS85 | |
A | LYS158 | |
A | LYS203 | |
A | LYS226 | |
A | LYS232 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
B | LYS200 | |
A | LYS75 | |
A | LYS101 | |
A | LYS139 | |
A | LYS164 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6,N6,N6-trimethyllysine; by ETFBKMT => ECO:0000269|PubMed:25023281, ECO:0000269|PubMed:25416781 |
Chain | Residue | Details |
B | LYS203 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DCW4 |
Chain | Residue | Details |
B | LYS210 | |
B | LYS248 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
B | SER223 | |
B | SER226 | |
A | LYS301 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCW4 |
Chain | Residue | Details |
B | LYS238 |