6RZE
Crystal structure of E. coli Adenylate kinase R119A mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004017 | molecular_function | adenylate kinase activity |
| A | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006172 | biological_process | ADP biosynthetic process |
| A | 0009123 | biological_process | nucleoside monophosphate metabolic process |
| A | 0009132 | biological_process | nucleoside diphosphate metabolic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0015951 | biological_process | purine ribonucleotide interconversion |
| A | 0016208 | molecular_function | AMP binding |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| A | 0044209 | biological_process | AMP salvage |
| A | 0046083 | biological_process | adenine metabolic process |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 301 |
| Chain | Residue |
| A | HOH404 |
| A | HOH481 |
| A | HOH545 |
| A | HOH619 |
| A | HOH656 |
| A | HOH710 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 302 |
| Chain | Residue |
| A | HOH739 |
| A | HOH555 |
| A | HOH561 |
| A | HOH628 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 303 |
| Chain | Residue |
| A | HOH534 |
| A | HOH574 |
| A | HOH663 |
| A | HOH752 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 304 |
| Chain | Residue |
| A | GLY10 |
| A | GLY12 |
| A | HOH613 |
| A | HOH669 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| A | ARG124 |
| A | LYS141 |
| A | GLY144 |
| A | ASP147 |
| A | HOH563 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtipQ |
| Chain | Residue | Details |
| A | PHE81-GLN92 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733, ECO:0000269|PubMed:8451239 |
| Chain | Residue | Details |
| A | GLY10 | |
| A | THR31 | |
| A | ARG36 | |
| A | LYS57 | |
| A | GLN92 | |
| A | ARG123 | |
| A | ARG156 | |
| A | LYS200 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:8451239 |
| Chain | Residue | Details |
| A | GLY85 | |
| A | ARG167 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16302237 |
| Chain | Residue | Details |
| A | ALA119 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:8451239 |
| Chain | Residue | Details |
| A | VAL132 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS192 |
