1AKE
STRUCTURE OF THE COMPLEX BETWEEN ADENYLATE KINASE FROM ESCHERICHIA COLI AND THE INHIBITOR AP5A REFINED AT 1.9 ANGSTROMS RESOLUTION: A MODEL FOR A CATALYTIC TRANSITION STATE
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 | 0016310 | biological_process | phosphorylation |
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 | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
A | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004017 | molecular_function | adenylate 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 | 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 | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
B | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
B | 0044209 | biological_process | AMP salvage |
B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
B | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 41 |
Details | BINDING SITE FOR RESIDUE AP5 A 215 |
Chain | Residue |
A | PRO9 |
A | MET53 |
A | LYS57 |
A | VAL59 |
A | VAL64 |
A | GLY85 |
A | PHE86 |
A | ARG88 |
A | GLN92 |
A | ARG119 |
A | ARG123 |
A | GLY10 |
A | VAL132 |
A | TYR133 |
A | HIS134 |
A | PHE137 |
A | ARG156 |
A | ARG167 |
A | LYS200 |
A | PRO201 |
A | VAL202 |
A | HOH303 |
A | ALA11 |
A | HOH304 |
A | HOH305 |
A | HOH307 |
A | HOH316 |
A | HOH320 |
A | HOH341 |
A | HOH355 |
A | HOH361 |
A | HOH362 |
A | HOH401 |
A | GLY12 |
A | HOH429 |
A | HOH456 |
A | LYS13 |
A | GLY14 |
A | THR15 |
A | THR31 |
A | ARG36 |
site_id | AC2 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE AP5 B 215 |
Chain | Residue |
B | PRO9 |
B | GLY10 |
B | ALA11 |
B | GLY12 |
B | LYS13 |
B | GLY14 |
B | THR15 |
B | THR31 |
B | LEU35 |
B | ARG36 |
B | MET53 |
B | LYS57 |
B | LEU58 |
B | VAL59 |
B | GLU62 |
B | VAL64 |
B | GLY85 |
B | ARG88 |
B | GLN92 |
B | ARG119 |
B | ARG123 |
B | VAL132 |
B | TYR133 |
B | HIS134 |
B | PHE137 |
B | ARG156 |
B | ASP158 |
B | ARG167 |
B | LYS200 |
B | VAL202 |
B | HOH603 |
B | HOH604 |
B | HOH605 |
B | HOH607 |
B | HOH620 |
B | HOH655 |
B | HOH666 |
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 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1zio |
Chain | Residue | Details |
A | LYS13 | |
A | ARG156 | |
A | ARG123 | |
A | ARG167 | |
A | ASP158 | |
A | ASP159 |
site_id | CSA2 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1zio |
Chain | Residue | Details |
B | LYS13 | |
B | ARG156 | |
B | ARG123 | |
B | ARG167 | |
B | ASP158 | |
B | ASP159 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1zio |
Chain | Residue | Details |
A | LYS13 | |
A | ARG123 | |
A | ASP33 | |
A | GLU162 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1zio |
Chain | Residue | Details |
B | LYS13 | |
B | ARG123 | |
B | ASP33 | |
B | GLU162 |