1EFV
THREE-DIMENSIONAL STRUCTURE OF HUMAN ELECTRON TRANSFER FLAVOPROTEIN TO 2.1 A RESOLUTION
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 | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A 599 |
| Chain | Residue |
| A | GLY222 |
| A | GLY264 |
| A | GLN265 |
| A | THR266 |
| A | GLY267 |
| A | GLY279 |
| A | ILE280 |
| A | SER281 |
| A | GLN285 |
| A | HIS286 |
| A | ASN300 |
| A | ARG223 |
| A | LYS301 |
| A | ASP302 |
| A | ALA317 |
| A | ASP318 |
| A | LEU319 |
| A | PHE320 |
| A | HOH1001 |
| A | HOH1102 |
| A | HOH1103 |
| A | HOH1166 |
| A | GLY224 |
| A | HOH1206 |
| A | HOH1251 |
| B | TYR16 |
| A | LYS226 |
| 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 | HOH1017 |
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. VeReiDGGl.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 |
