5E4H
Crystal Structure of Apoenzyme Alpha-kinase Domain of Myosin-II Heavy Chain Kinase A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004674 | molecular_function | protein serine/threonine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004674 | molecular_function | protein serine/threonine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
E | 0004674 | molecular_function | protein serine/threonine kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006468 | biological_process | protein phosphorylation |
F | 0004674 | molecular_function | protein serine/threonine kinase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006468 | biological_process | protein phosphorylation |
G | 0004674 | molecular_function | protein serine/threonine kinase activity |
G | 0005524 | molecular_function | ATP binding |
G | 0006468 | biological_process | protein phosphorylation |
H | 0004674 | molecular_function | protein serine/threonine kinase activity |
H | 0005524 | molecular_function | ATP binding |
H | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 901 |
Chain | Residue |
A | HIS742 |
A | HIS794 |
A | CYS796 |
A | CYS800 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN B 901 |
Chain | Residue |
B | HIS742 |
B | HIS794 |
B | CYS796 |
B | CYS800 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN C 901 |
Chain | Residue |
C | HIS794 |
C | CYS796 |
C | CYS800 |
C | HIS742 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN D 901 |
Chain | Residue |
D | HIS742 |
D | HIS794 |
D | CYS796 |
D | CYS800 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN E 901 |
Chain | Residue |
E | HIS742 |
E | HIS794 |
E | CYS796 |
E | CYS800 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue ZN F 901 |
Chain | Residue |
F | HIS742 |
F | HIS794 |
F | CYS796 |
F | CYS800 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN G 901 |
Chain | Residue |
G | HIS742 |
G | HIS794 |
G | CYS796 |
G | CYS800 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue ZN H 901 |
Chain | Residue |
H | HIS742 |
H | HIS794 |
H | CYS796 |
H | CYS800 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
B | GLY778 | |
C | GLY778 | |
D | GLY778 | |
E | GLY778 | |
F | GLY778 | |
G | GLY778 | |
H | GLY778 | |
A | GLY778 |