3AKY
STABILITY, ACTIVITY AND STRUCTURE OF ADENYLATE KINASE MUTANTS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003688 | molecular_function | DNA replication origin binding |
A | 0004017 | molecular_function | adenylate kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005758 | cellular_component | mitochondrial intermembrane space |
A | 0005829 | cellular_component | cytosol |
A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0006172 | biological_process | ADP biosynthetic process |
A | 0006270 | biological_process | DNA replication initiation |
A | 0009117 | biological_process | nucleotide metabolic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
A | 0036388 | biological_process | pre-replicative complex assembly |
A | 0046033 | biological_process | AMP metabolic process |
A | 0046034 | biological_process | ATP metabolic process |
A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 40 |
Details | BINDING SITE FOR RESIDUE AP5 A 301 |
Chain | Residue |
A | PRO13 |
A | ARG40 |
A | MET57 |
A | GLY61 |
A | VAL63 |
A | MET68 |
A | GLY90 |
A | PHE91 |
A | ARG93 |
A | GLN97 |
A | ARG128 |
A | GLY14 |
A | ARG132 |
A | SER141 |
A | TYR142 |
A | HIS143 |
A | PHE146 |
A | ARG165 |
A | ARG176 |
A | GLN204 |
A | PRO205 |
A | PRO206 |
A | ALA15 |
A | IMD302 |
A | HOH501 |
A | HOH504 |
A | HOH506 |
A | HOH517 |
A | HOH530 |
A | HOH536 |
A | HOH541 |
A | HOH570 |
A | HOH587 |
A | GLY16 |
A | HOH600 |
A | LYS17 |
A | GLY18 |
A | THR19 |
A | THR35 |
A | GLY36 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE IMD A 302 |
Chain | Residue |
A | GLY18 |
A | ASP37 |
A | ASP89 |
A | AP5301 |
A | HOH541 |
A | HOH587 |
A | HOH621 |
Functional Information from PROSITE/UniProt
site_id | PS00113 |
Number of Residues | 12 |
Details | ADENYLATE_KINASE Adenylate kinase signature. FILDGFPRtipQ |
Chain | Residue | Details |
A | PHE86-GLN97 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191 |
Chain | Residue | Details |
A | GLY14 | |
A | ARG132 | |
A | GLN204 |
site_id | SWS_FT_FI2 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369 |
Chain | Residue | Details |
A | THR35 | |
A | ARG40 | |
A | GLY61 | |
A | GLY90 | |
A | GLN97 | |
A | ARG165 | |
A | ARG176 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191 |
Chain | Residue | Details |
A | SER141 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:3004985 |
Chain | Residue | Details |
A | SER1 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1zio |
Chain | Residue | Details |
A | LYS17 | |
A | ASP167 | |
A | ARG165 | |
A | ARG176 | |
A | ARG132 | |
A | ASP168 |