1DVR
STRUCTURE OF A MUTANT ADENYLATE KINASE LIGATED WITH AN ATP-ANALOGUE SHOWING DOMAIN CLOSURE OVER ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003688 | molecular_function | DNA replication origin binding |
| A | 0004017 | molecular_function | AMP kinase activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0016208 | molecular_function | AMP binding |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003688 | molecular_function | DNA replication origin binding |
| B | 0004017 | molecular_function | AMP kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005758 | cellular_component | mitochondrial intermembrane space |
| B | 0005829 | cellular_component | cytosol |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0006172 | biological_process | ADP biosynthetic process |
| B | 0006270 | biological_process | DNA replication initiation |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0016208 | molecular_function | AMP binding |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| B | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| B | 0036388 | biological_process | pre-replicative complex assembly |
| B | 0046033 | biological_process | AMP metabolic process |
| B | 0046034 | biological_process | ATP metabolic process |
| B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ATF A 230 |
| Chain | Residue |
| A | PRO13 |
| A | SER141 |
| A | TYR142 |
| A | HIS143 |
| A | PHE146 |
| A | ALA202 |
| A | GLN204 |
| A | PRO206 |
| A | HOH243 |
| A | HOH249 |
| A | HOH252 |
| A | GLY14 |
| A | HOH291 |
| B | LYS55 |
| B | GLN59 |
| B | HOH231 |
| A | ALA15 |
| A | GLY16 |
| A | LYS17 |
| A | GLY18 |
| A | THR19 |
| A | ARG128 |
| A | ARG132 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATF B 230 |
| Chain | Residue |
| A | LYS55 |
| A | GLN59 |
| B | PRO13 |
| B | GLY14 |
| B | GLY16 |
| B | LYS17 |
| B | GLY18 |
| B | THR19 |
| B | ARG128 |
| B | ARG132 |
| B | SER141 |
| B | TYR142 |
| B | HIS143 |
| B | PHE146 |
| B | GLN204 |
| B | PRO205 |
| B | PRO206 |
| B | HOH261 |
| B | HOH289 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_03168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7635152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7670369","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 74 |
| Details | Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_03168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7635152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7670369","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7635152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7670369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8594191","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7635152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7670369","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7635152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7670369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8594191","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"HAMAP-Rule","id":"MF_03168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3004985","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
