4X8O
Crystal structure of E. coli Adenylate kinase Y171W mutant in complex with inhibitor Ap5a
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004017 | molecular_function | adenylate kinase activity |
A | 0004127 | molecular_function | cytidylate 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 | 0006225 | biological_process | UDP 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 | 0016310 | biological_process | phosphorylation |
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 | 0033862 | molecular_function | UMP kinase activity |
A | 0044209 | biological_process | AMP salvage |
A | 0046705 | biological_process | CDP biosynthetic process |
A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
A | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
A | 1901566 | biological_process | organonitrogen compound biosynthetic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004017 | molecular_function | adenylate kinase activity |
B | 0004127 | molecular_function | cytidylate kinase activity |
B | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
B | 0006172 | biological_process | ADP biosynthetic process |
B | 0006225 | biological_process | UDP biosynthetic process |
B | 0009123 | biological_process | nucleoside monophosphate metabolic process |
B | 0009132 | biological_process | nucleoside diphosphate metabolic process |
B | 0009165 | biological_process | nucleotide biosynthetic process |
B | 0015951 | biological_process | purine ribonucleotide interconversion |
B | 0016208 | molecular_function | AMP binding |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
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 | 0033862 | molecular_function | UMP kinase activity |
B | 0044209 | biological_process | AMP salvage |
B | 0046705 | biological_process | CDP biosynthetic process |
B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
B | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
B | 1901566 | biological_process | organonitrogen compound biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 39 |
Details | binding site for residue AP5 A 301 |
Chain | Residue |
A | PRO9 |
A | LEU35 |
A | ARG36 |
A | MET53 |
A | LYS57 |
A | VAL59 |
A | GLU62 |
A | VAL64 |
A | GLY85 |
A | ARG88 |
A | GLN92 |
A | GLY10 |
A | ARG119 |
A | ARG123 |
A | VAL132 |
A | TYR133 |
A | HIS134 |
A | PHE137 |
A | ARG156 |
A | ARG167 |
A | GLY198 |
A | LYS200 |
A | ALA11 |
A | VAL202 |
A | MG302 |
A | HOH435 |
A | HOH460 |
A | HOH462 |
A | HOH478 |
A | HOH530 |
A | HOH557 |
A | HOH558 |
A | HOH579 |
A | GLY12 |
A | LYS13 |
A | GLY14 |
A | THR15 |
A | THR31 |
A | GLY32 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue MG A 302 |
Chain | Residue |
A | GLY14 |
A | ASP84 |
A | AP5301 |
A | HOH579 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue NA A 303 |
Chain | Residue |
A | VAL103 |
A | ASN190 |
A | HOH417 |
A | HOH444 |
A | HOH452 |
site_id | AC4 |
Number of Residues | 40 |
Details | binding site for residue AP5 B 301 |
Chain | Residue |
B | PRO9 |
B | GLY10 |
B | ALA11 |
B | GLY12 |
B | LYS13 |
B | GLY14 |
B | THR15 |
B | THR31 |
B | GLY32 |
B | LEU35 |
B | ARG36 |
B | MET53 |
B | LYS57 |
B | LEU58 |
B | VAL59 |
B | VAL64 |
B | GLY85 |
B | PHE86 |
B | ARG88 |
B | GLN92 |
B | ARG119 |
B | ARG123 |
B | TYR133 |
B | HIS134 |
B | PHE137 |
B | ARG156 |
B | ASP158 |
B | ARG167 |
B | LYS200 |
B | VAL202 |
B | MG302 |
B | HOH429 |
B | HOH458 |
B | HOH460 |
B | HOH484 |
B | HOH518 |
B | HOH530 |
B | HOH531 |
B | HOH532 |
B | HOH535 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue MG B 302 |
Chain | Residue |
B | ASP84 |
B | AP5301 |
B | HOH534 |
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 | 16 |
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 | |
B | THR31 | |
B | ARG36 | |
B | LYS57 | |
B | GLN92 | |
B | ARG123 | |
B | ARG156 | |
B | LYS200 | |
A | THR31 | |
A | ARG36 | |
A | LYS57 | |
A | GLN92 | |
A | ARG123 | |
A | ARG156 | |
A | LYS200 | |
B | GLY10 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
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 | |
B | GLY85 | |
B | ARG167 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16302237 |
Chain | Residue | Details |
A | ARG119 | |
B | ARG119 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
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 | |
B | VAL132 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | LYS192 | |
B | LYS192 |