6DZG
Crystal structure of polyphosphate kinase 2 class I (SMc02148) in complex with ADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006754 | biological_process | ATP biosynthetic process |
A | 0006793 | biological_process | phosphorus metabolic process |
A | 0008976 | molecular_function | polyphosphate kinase activity |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0042802 | molecular_function | identical protein binding |
B | 0006754 | biological_process | ATP biosynthetic process |
B | 0006793 | biological_process | phosphorus metabolic process |
B | 0008976 | molecular_function | polyphosphate kinase activity |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0042802 | molecular_function | identical protein binding |
C | 0006754 | biological_process | ATP biosynthetic process |
C | 0006793 | biological_process | phosphorus metabolic process |
C | 0008976 | molecular_function | polyphosphate kinase activity |
C | 0016301 | molecular_function | kinase activity |
C | 0016310 | biological_process | phosphorylation |
C | 0042802 | molecular_function | identical protein binding |
D | 0006754 | biological_process | ATP biosynthetic process |
D | 0006793 | biological_process | phosphorus metabolic process |
D | 0008976 | molecular_function | polyphosphate kinase activity |
D | 0016301 | molecular_function | kinase activity |
D | 0016310 | biological_process | phosphorylation |
D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue ADP A 401 |
Chain | Residue |
A | LYS97 |
A | HOH547 |
A | HOH564 |
B | ASN109 |
B | ARG111 |
A | LYS120 |
A | ARG149 |
A | ASN153 |
A | PHE163 |
A | SER220 |
A | MSE222 |
A | HOH516 |
A | HOH529 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue MLT A 402 |
Chain | Residue |
A | ALA94 |
A | GLY96 |
A | LYS97 |
A | GLY98 |
A | GLY99 |
A | ARG209 |
A | LYS218 |
site_id | AC3 |
Number of Residues | 13 |
Details | binding site for residue ADP B 401 |
Chain | Residue |
A | ARG111 |
B | LYS120 |
B | ARG149 |
B | ASN153 |
B | VAL157 |
B | PHE163 |
B | SER220 |
B | MSE222 |
B | HOH503 |
B | HOH509 |
B | HOH526 |
B | HOH536 |
B | HOH568 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue MLT B 402 |
Chain | Residue |
B | ALA94 |
B | ALA95 |
B | GLY96 |
B | LYS97 |
B | GLY98 |
B | GLY99 |
B | ARG209 |
B | LYS218 |
B | HOH571 |
B | HOH580 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue MLT B 403 |
Chain | Residue |
B | GLU59 |
B | ARG261 |
B | ARG268 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue ADP C 401 |
Chain | Residue |
C | LYS120 |
C | ARG149 |
C | ASN153 |
C | PHE163 |
C | SER220 |
C | MSE222 |
C | HOH510 |
C | HOH534 |
C | HOH547 |
C | HOH576 |
D | ASN109 |
D | ARG111 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue MLT C 402 |
Chain | Residue |
C | ALA94 |
C | GLY96 |
C | LYS97 |
C | GLY98 |
C | GLY99 |
C | ARG209 |
C | LYS218 |
site_id | AC8 |
Number of Residues | 13 |
Details | binding site for residue AMP D 401 |
Chain | Residue |
C | ARG111 |
D | LYS120 |
D | ARG149 |
D | ASN153 |
D | PHE163 |
D | SER220 |
D | MSE222 |
D | HOH550 |
D | HOH559 |
D | HOH560 |
D | HOH570 |
D | HOH613 |
D | HOH622 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue MLT D 402 |
Chain | Residue |
D | ALA94 |
D | GLY96 |
D | LYS97 |
D | GLY98 |
D | GLY99 |
D | ARG209 |
D | LYS218 |