5LDB
Crystal Structure of Polyphosphate Kinase from Meiothermus ruber bound to ADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006797 | biological_process | polyphosphate metabolic process |
A | 0008976 | molecular_function | polyphosphate kinase activity |
A | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
B | 0006797 | biological_process | polyphosphate metabolic process |
B | 0008976 | molecular_function | polyphosphate kinase activity |
B | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
C | 0006797 | biological_process | polyphosphate metabolic process |
C | 0008976 | molecular_function | polyphosphate kinase activity |
C | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
D | 0006797 | biological_process | polyphosphate metabolic process |
D | 0008976 | molecular_function | polyphosphate kinase activity |
D | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue ADP A 1001 |
Chain | Residue |
A | LYS70 |
A | VAL130 |
A | ARG193 |
A | MG1003 |
A | HOH1119 |
A | HOH1123 |
A | HOH1150 |
A | HOH1162 |
A | HOH1200 |
A | PHE91 |
A | GLY92 |
A | VAL93 |
A | PRO94 |
A | ARG106 |
A | ARG122 |
A | GLU126 |
A | ASP127 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue PO4 A 1002 |
Chain | Residue |
A | ALA67 |
A | GLY68 |
A | GLY69 |
A | LYS70 |
A | ASP71 |
A | ARG182 |
A | HOH1119 |
A | HOH1121 |
A | HOH1162 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue MG A 1003 |
Chain | Residue |
A | LYS191 |
A | ADP1001 |
A | HOH1123 |
A | HOH1171 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL A 1004 |
Chain | Residue |
A | GLY72 |
A | ARG75 |
A | ASN232 |
A | ARG235 |
A | ASN236 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue ADP B 1001 |
Chain | Residue |
B | LYS70 |
B | PHE91 |
B | GLY92 |
B | VAL93 |
B | PRO94 |
B | ARG106 |
B | ARG122 |
B | GLU126 |
B | ASP127 |
B | VAL130 |
B | MG1003 |
B | HOH1167 |
B | HOH1182 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue PO4 B 1002 |
Chain | Residue |
B | ALA67 |
B | GLY68 |
B | GLY69 |
B | LYS70 |
B | ASP71 |
B | ARG182 |
B | HOH1145 |
B | HOH1190 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue MG B 1003 |
Chain | Residue |
B | ADP1001 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue CL B 1004 |
Chain | Residue |
B | LYS29 |
B | TRP233 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue ADP C 1001 |
Chain | Residue |
C | LYS70 |
C | PHE91 |
C | GLY92 |
C | VAL93 |
C | PRO94 |
C | ARG106 |
C | ARG122 |
C | GLU126 |
C | ASP127 |
C | VAL130 |
C | ARG193 |
C | HOH1159 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue PO4 C 1002 |
Chain | Residue |
C | ALA67 |
C | GLY68 |
C | GLY69 |
C | LYS70 |
C | ASP71 |
C | ARG182 |
C | HOH1127 |
C | HOH1159 |
site_id | AD2 |
Number of Residues | 15 |
Details | binding site for residue ADP D 1001 |
Chain | Residue |
D | LYS70 |
D | PHE91 |
D | GLY92 |
D | VAL93 |
D | PRO94 |
D | ARG106 |
D | ARG122 |
D | GLU126 |
D | ASP127 |
D | VAL130 |
D | ARG193 |
D | MG1003 |
D | HOH1111 |
D | HOH1151 |
D | HOH1153 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue PO4 D 1002 |
Chain | Residue |
D | ARG182 |
D | HOH1111 |
D | HOH1163 |
D | ALA67 |
D | GLY68 |
D | GLY69 |
D | LYS70 |
D | ASP71 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue MG D 1003 |
Chain | Residue |
D | ASP196 |
D | ADP1001 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue MG D 1004 |
Chain | Residue |
B | THR95 |
B | GLN97 |
B | HOH1236 |
D | THR95 |
D | GLN97 |