Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0005524 | molecular_function | ATP binding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0005524 | molecular_function | ATP binding |
C | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0005524 | molecular_function | ATP binding |
D | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0005524 | molecular_function | ATP binding |
E | 0016887 | molecular_function | ATP hydrolysis activity |
E | 0046872 | molecular_function | metal ion binding |
F | 0005524 | molecular_function | ATP binding |
F | 0016887 | molecular_function | ATP hydrolysis activity |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue ADP A 401 |
Chain | Residue |
A | LEU110 |
A | GLU164 |
A | LEU269 |
A | ARG278 |
A | LEU280 |
A | HOH501 |
A | PRO132 |
A | THR133 |
A | GLY134 |
A | SER135 |
A | GLY136 |
A | LYS137 |
A | SER138 |
A | THR139 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue ADP B 401 |
Chain | Residue |
B | LEU110 |
B | PRO132 |
B | THR133 |
B | GLY134 |
B | SER135 |
B | GLY136 |
B | LYS137 |
B | SER138 |
B | THR139 |
B | LEU269 |
B | ARG278 |
B | LEU280 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue ADP C 401 |
Chain | Residue |
C | LEU110 |
C | PRO132 |
C | THR133 |
C | GLY134 |
C | SER135 |
C | GLY136 |
C | LYS137 |
C | SER138 |
C | THR139 |
C | GLU164 |
C | LEU269 |
C | ARG278 |
C | LEU280 |
C | HOH501 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue ADP E 401 |
Chain | Residue |
E | LEU110 |
E | PRO132 |
E | THR133 |
E | GLY134 |
E | SER135 |
E | GLY136 |
E | LYS137 |
E | SER138 |
E | THR139 |
E | GLU164 |
E | LEU269 |
E | ARG278 |
E | LEU280 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for Di-peptide ADP D 401 and GLY D 134 |
Chain | Residue |
D | LEU110 |
D | PRO132 |
D | THR133 |
D | SER135 |
D | GLY136 |
D | LYS137 |
D | SER138 |
D | THR139 |
D | GLU164 |
D | LEU269 |
D | ARG278 |
D | LEU280 |
D | HOH501 |
site_id | AC6 |
Number of Residues | 16 |
Details | binding site for Di-peptide ADP F 401 and LYS F 137 |
Chain | Residue |
F | ARG98 |
F | LEU110 |
F | VAL129 |
F | THR130 |
F | GLY131 |
F | PRO132 |
F | THR133 |
F | GLY134 |
F | SER135 |
F | GLY136 |
F | SER138 |
F | THR139 |
F | THR140 |
F | LEU141 |
F | LEU269 |
F | LEU280 |
Functional Information from PROSITE/UniProt
site_id | PS00662 |
Number of Residues | 15 |
Details | T2SP_E Bacterial type II secretion system protein E signature. LRqdPDvVLVGELRD |
Chain | Residue | Details |
A | LEU194-ASP208 | |