Functional Information from GO Data
Chain | GOid | namespace | contents |
1 | 0005524 | molecular_function | ATP binding |
1 | 0016887 | molecular_function | ATP hydrolysis activity |
2 | 0005524 | molecular_function | ATP binding |
2 | 0016887 | molecular_function | ATP hydrolysis activity |
3 | 0005524 | molecular_function | ATP binding |
3 | 0016887 | molecular_function | ATP hydrolysis activity |
4 | 0005524 | molecular_function | ATP binding |
4 | 0016887 | molecular_function | ATP hydrolysis activity |
5 | 0005524 | molecular_function | ATP binding |
5 | 0016887 | molecular_function | ATP hydrolysis activity |
6 | 0005524 | molecular_function | ATP binding |
6 | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue AGS 1 1001 |
Chain | Residue |
1 | ASN227 |
2 | THR242 |
2 | THR243 |
2 | LEU382 |
2 | ILE420 |
1 | SER333 |
1 | ARG360 |
1 | ARG361 |
2 | PRO237 |
2 | GLY238 |
2 | THR239 |
2 | GLY240 |
2 | LYS241 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue AGS 1 1002 |
Chain | Residue |
1 | PRO237 |
1 | THR239 |
1 | GLY240 |
1 | LYS241 |
1 | THR242 |
1 | THR243 |
1 | ASP417 |
1 | ILE420 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue AGS 1 1003 |
Chain | Residue |
1 | SER602 |
1 | ILE603 |
1 | GLY641 |
1 | VAL642 |
1 | GLY643 |
1 | LYS644 |
1 | THR645 |
1 | GLU646 |
1 | ASN752 |
1 | ARG859 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue AGS 2 1001 |
Chain | Residue |
1 | ARG800 |
2 | GLY641 |
2 | VAL642 |
2 | GLY643 |
2 | LYS644 |
2 | THR645 |
2 | GLU646 |
2 | ASN752 |
2 | ARG822 |
2 | ARG859 |
2 | LEU862 |
site_id | AC5 |
Number of Residues | 15 |
Details | binding site for residue AGS 3 1002 |
Chain | Residue |
2 | GLU796 |
2 | ARG800 |
3 | SER602 |
3 | THR640 |
3 | GLY641 |
3 | VAL642 |
3 | GLY643 |
3 | LYS644 |
3 | THR645 |
3 | GLU646 |
3 | ASN752 |
3 | ILE818 |
3 | ARG822 |
3 | ARG859 |
3 | LEU862 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue AGS 4 1002 |
Chain | Residue |
4 | SER602 |
4 | ILE603 |
4 | GLY641 |
4 | VAL642 |
4 | GLY643 |
4 | LYS644 |
4 | THR645 |
4 | GLU646 |
4 | GLU711 |
4 | ARG859 |
site_id | AC7 |
Number of Residues | 12 |
Details | binding site for residue AGS 5 1001 |
Chain | Residue |
4 | ARG360 |
5 | TYR210 |
5 | PRO237 |
5 | GLY238 |
5 | THR239 |
5 | GLY240 |
5 | LYS241 |
5 | THR242 |
5 | THR243 |
5 | ILE378 |
5 | LEU382 |
5 | ASP417 |
site_id | AC8 |
Number of Residues | 13 |
Details | binding site for residue AGS 5 1002 |
Chain | Residue |
4 | ARG800 |
5 | ILE603 |
5 | ILE604 |
5 | GLY605 |
5 | GLY641 |
5 | VAL642 |
5 | GLY643 |
5 | LYS644 |
5 | THR645 |
5 | GLU646 |
5 | ILE818 |
5 | ARG859 |
5 | LEU862 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DDDDDDDLDedEF |
Chain | Residue | Details |
d | ASP668 | |
site_id | PS00870 |
Number of Residues | 13 |
Details | CLPAB_1 Chaperonins clpA/B signature 1. DAANLLKPvLskG |
Chain | Residue | Details |
1 | ASP323-GLY335 | |
site_id | PS00871 |
Number of Residues | 19 |
Details | CLPAB_2 Chaperonins clpA/B signature 2. RVNmSEFtEAhSvSKItGS |
Chain | Residue | Details |
1 | ARG664-SER682 | |