3JU5
Crystal Structure of Dimeric Arginine Kinase at 1.75-A Resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004054 | molecular_function | arginine kinase activity |
A | 0004111 | molecular_function | creatine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0016301 | molecular_function | kinase activity |
A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
A | 0046314 | biological_process | phosphocreatine biosynthetic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0004054 | molecular_function | arginine kinase activity |
B | 0004111 | molecular_function | creatine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0016301 | molecular_function | kinase activity |
B | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
B | 0046314 | biological_process | phosphocreatine biosynthetic process |
C | 0003824 | molecular_function | catalytic activity |
C | 0004054 | molecular_function | arginine kinase activity |
C | 0004111 | molecular_function | creatine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0016301 | molecular_function | kinase activity |
C | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
C | 0046314 | biological_process | phosphocreatine biosynthetic process |
D | 0003824 | molecular_function | catalytic activity |
D | 0004054 | molecular_function | arginine kinase activity |
D | 0004111 | molecular_function | creatine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0016301 | molecular_function | kinase activity |
D | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
D | 0046314 | biological_process | phosphocreatine biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 371 |
Chain | Residue |
A | ALA2 |
A | ARG50 |
A | HOH1139 |
B | HOH1007 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 371 |
Chain | Residue |
C | ALA2 |
C | ARG50 |
C | HOH414 |
Functional Information from PROSITE/UniProt
site_id | PS00112 |
Number of Residues | 7 |
Details | PHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.SNLGT |
Chain | Residue | Details |
A | CYS274-THR280 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00843 |
Chain | Residue | Details |
A | SER118 | |
B | ARG311 | |
C | SER118 | |
C | HIS181 | |
C | ARG226 | |
C | ARG283 | |
C | ARG311 | |
D | SER118 | |
D | HIS181 | |
D | ARG226 | |
D | ARG283 | |
A | HIS181 | |
D | ARG311 | |
A | ARG226 | |
A | ARG283 | |
A | ARG311 | |
B | SER118 | |
B | HIS181 | |
B | ARG226 | |
B | ARG283 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLU222 | |
D | GLU222 | |
D | CYS274 | |
D | GLU316 | |
A | CYS274 | |
A | GLU316 | |
B | GLU222 | |
B | CYS274 | |
B | GLU316 | |
C | GLU222 | |
C | CYS274 | |
C | GLU316 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1bg0 |
Chain | Residue | Details |
A | ARG226 | |
A | ARG122 | |
A | GLU222 | |
A | ARG283 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1bg0 |
Chain | Residue | Details |
B | ARG226 | |
B | ARG122 | |
B | GLU222 | |
B | ARG283 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1bg0 |
Chain | Residue | Details |
C | ARG226 | |
C | ARG122 | |
C | GLU222 | |
C | ARG283 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1bg0 |
Chain | Residue | Details |
D | ARG226 | |
D | ARG122 | |
D | GLU222 | |
D | ARG283 |