4YMU
Crystal structure of an amino acid ABC transporter complex with arginines and ATPs
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003333 | biological_process | amino acid transmembrane transport |
| A | 0005524 | molecular_function | ATP binding |
| A | 0015424 | molecular_function | ABC-type amino acid transporter activity |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0046872 | molecular_function | metal ion binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006865 | biological_process | amino acid transport |
| C | 0016020 | cellular_component | membrane |
| C | 0022857 | molecular_function | transmembrane transporter activity |
| C | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
| C | 0055085 | biological_process | transmembrane transport |
| C | 0071705 | biological_process | nitrogen compound transport |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006865 | biological_process | amino acid transport |
| D | 0016020 | cellular_component | membrane |
| D | 0022857 | molecular_function | transmembrane transporter activity |
| D | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
| D | 0055085 | biological_process | transmembrane transport |
| D | 0071705 | biological_process | nitrogen compound transport |
| J | 0000166 | molecular_function | nucleotide binding |
| J | 0003333 | biological_process | amino acid transmembrane transport |
| J | 0005524 | molecular_function | ATP binding |
| J | 0015424 | molecular_function | ABC-type amino acid transporter activity |
| J | 0016887 | molecular_function | ATP hydrolysis activity |
| J | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue ATP J 301 |
| Chain | Residue |
| J | PHE11 |
| J | GLU51 |
| J | GLU162 |
| J | HIS194 |
| J | MG302 |
| J | VAL16 |
| J | SER36 |
| J | GLY37 |
| J | SER38 |
| J | GLY39 |
| J | LYS40 |
| J | SER41 |
| J | THR42 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG J 302 |
| Chain | Residue |
| J | SER41 |
| J | GLU162 |
| J | ATP301 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue ATP A 301 |
| Chain | Residue |
| A | PHE11 |
| A | VAL16 |
| A | SER36 |
| A | GLY37 |
| A | SER38 |
| A | GLY39 |
| A | LYS40 |
| A | SER41 |
| A | THR42 |
| A | GLU51 |
| A | GLU162 |
| A | HIS194 |
| A | MG302 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | SER41 |
| A | GLU162 |
| A | ATP301 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue ARG D 301 |
| Chain | Residue |
| C | LYS158 |
| C | GLU159 |
| C | ARG301 |
| D | LEU67 |
| D | ASN98 |
| D | TYR102 |
| D | GLU152 |
| D | MET156 |
| D | GLU159 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue ARG C 301 |
| Chain | Residue |
| C | PRO66 |
| C | LEU67 |
| C | ASN98 |
| C | TYR102 |
| C | GLU152 |
| C | MET156 |
| C | GLU159 |
| D | LYS158 |
| D | GLU159 |
| D | ARG301 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for Ligand LEU C 206 bound to THR C 202 |
| Chain | Residue |
| C | THR202 |
| C | PHE203 |
| C | SER204 |
| C | LYS205 |
| C | LEU207 |
| C | SER208 |
| C | LEU209 |
| C | PHE210 |
Functional Information from PROSITE/UniProt
| site_id | PS00211 |
| Number of Residues | 15 |
| Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRLAIARAL |
| Chain | Residue | Details |
| J | LEU137-LEU151 |
