1O96
Structure of electron transferring flavoprotein for Methylophilus methylotrophus.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0009055 | molecular_function | electron transfer activity |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0009055 | molecular_function | electron transfer activity |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0009055 | molecular_function | electron transfer activity |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| Q | 0000166 | molecular_function | nucleotide binding |
| Q | 0009055 | molecular_function | electron transfer activity |
| Z | 0009055 | molecular_function | electron transfer activity |
| Z | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| Z | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AMP A1263 |
| Chain | Residue |
| A | ALA6 |
| A | SER122 |
| A | TYR127 |
| A | ALA128 |
| A | SER129 |
| A | THR130 |
| A | VAL7 |
| A | LYS8 |
| A | ASN36 |
| A | ASP39 |
| A | VAL64 |
| A | ALA118 |
| A | GLY119 |
| A | GLN121 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD B1319 |
| Chain | Residue |
| A | TRP38 |
| A | GLN121 |
| A | GLN183 |
| B | GLY209 |
| B | ARG210 |
| B | GLY211 |
| B | SER235 |
| B | ARG236 |
| B | PRO237 |
| B | GLN249 |
| B | VAL250 |
| B | GLY251 |
| B | GLN252 |
| B | SER253 |
| B | GLY267 |
| B | SER269 |
| B | SER271 |
| B | GLN273 |
| B | HIS274 |
| B | ASN288 |
| B | THR289 |
| B | ASP290 |
| B | ALA305 |
| B | ASP306 |
| B | ILE307 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AMP C1262 |
| Chain | Residue |
| C | ALA6 |
| C | VAL7 |
| C | LYS8 |
| C | ASN36 |
| C | ASP39 |
| C | VAL62 |
| C | SER63 |
| C | VAL64 |
| C | VAL100 |
| C | LEU104 |
| C | ALA118 |
| C | GLY119 |
| C | GLN121 |
| C | SER122 |
| C | TYR127 |
| C | ALA128 |
| C | SER129 |
| C | THR130 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD D1319 |
| Chain | Residue |
| C | GLN121 |
| C | GLN183 |
| D | GLY209 |
| D | ARG210 |
| D | SER235 |
| D | ARG236 |
| D | PRO237 |
| D | GLN249 |
| D | VAL250 |
| D | GLY251 |
| D | GLN252 |
| D | SER253 |
| D | GLY254 |
| D | GLY267 |
| D | ILE268 |
| D | SER269 |
| D | SER271 |
| D | GLN273 |
| D | HIS274 |
| D | ASN288 |
| D | THR289 |
| D | ASP290 |
| D | ALA305 |
| D | ASP306 |
| D | ILE307 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AMP E1262 |
| Chain | Residue |
| E | ALA6 |
| E | VAL7 |
| E | LYS8 |
| E | ASN36 |
| E | ASP39 |
| E | VAL62 |
| E | SER63 |
| E | VAL64 |
| E | VAL100 |
| E | ALA118 |
| E | GLY119 |
| E | GLN121 |
| E | SER122 |
| E | TYR127 |
| E | ALA128 |
| E | SER129 |
| E | THR130 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD F1319 |
| Chain | Residue |
| E | GLN121 |
| E | GLN183 |
| F | GLY209 |
| F | ARG210 |
| F | GLY211 |
| F | SER235 |
| F | ARG236 |
| F | PRO237 |
| F | GLN249 |
| F | VAL250 |
| F | GLY251 |
| F | GLN252 |
| F | SER253 |
| F | GLY254 |
| F | GLY267 |
| F | SER269 |
| F | SER271 |
| F | GLN273 |
| F | HIS274 |
| F | ASN288 |
| F | THR289 |
| F | ASP290 |
| F | ALA305 |
| F | ASP306 |
| F | ILE307 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AMP Q1262 |
| Chain | Residue |
| Q | ALA6 |
| Q | VAL7 |
| Q | LYS8 |
| Q | ASN36 |
| Q | ASP39 |
| Q | VAL62 |
| Q | SER63 |
| Q | VAL64 |
| Q | VAL100 |
| Q | ALA118 |
| Q | GLY119 |
| Q | GLN121 |
| Q | SER122 |
| Q | TYR127 |
| Q | ALA128 |
| Q | SER129 |
| Q | THR130 |
| site_id | AC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD Z1319 |
| Chain | Residue |
| Q | GLN183 |
| Q | LEU184 |
| Z | GLY209 |
| Z | ARG210 |
| Z | SER235 |
| Z | ARG236 |
| Z | PRO237 |
| Z | GLN249 |
| Z | VAL250 |
| Z | GLY251 |
| Z | GLN252 |
| Z | SER253 |
| Z | GLY254 |
| Z | GLY267 |
| Z | SER269 |
| Z | SER271 |
| Z | GLN273 |
| Z | HIS274 |
| Z | ASN288 |
| Z | THR289 |
| Z | ASP290 |
| Z | ALA305 |
| Z | ILE307 |
Functional Information from PROSITE/UniProt
| site_id | PS00696 |
| Number of Residues | 27 |
| Details | ETF_ALPHA Electron transfer flavoprotein alpha-subunit signature. LYVAmGISGsIQHmaGmkhvptIiAVN |
| Chain | Residue | Details |
| B | LEU262-ASN288 |
| site_id | PS01065 |
| Number of Residues | 22 |
| Details | ETF_BETA Electron transfer flavoprotein beta-subunit signature. IrRelEGGmlQeVeincPaVLT |
| Chain | Residue | Details |
| A | ILE160-THR181 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12567183, ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR, ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU |
| Chain | Residue | Details |
| B | GLY211 | |
| D | ILE268 | |
| D | THR289 | |
| D | ILE307 | |
| F | GLY211 | |
| F | ARG236 | |
| F | VAL250 | |
| F | ILE268 | |
| F | THR289 | |
| F | ILE307 | |
| Z | GLY211 | |
| B | ARG236 | |
| Z | ARG236 | |
| Z | VAL250 | |
| Z | ILE268 | |
| Z | THR289 | |
| Z | ILE307 | |
| B | VAL250 | |
| B | ILE268 | |
| B | THR289 | |
| B | ILE307 | |
| D | GLY211 | |
| D | ARG236 | |
| D | VAL250 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: 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 |
| Chain | Residue | Details |
| A | VAL64 | |
| C | VAL64 | |
| E | VAL64 | |
| Q | VAL64 |
