3ADK
REFINED STRUCTURE OF PORCINE CYTOSOLIC ADENYLATE KINASE AT 2.1 ANGSTROMS RESOLUTION
Replaces: 2ADKReplaces: 1ADKFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004017 | molecular_function | AMP kinase activity |
| A | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006172 | biological_process | ADP biosynthetic process |
| A | 0009142 | biological_process | nucleoside triphosphate biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| A | 0046033 | biological_process | AMP metabolic process |
| A | 0046034 | biological_process | ATP metabolic process |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| A | 0047506 | molecular_function | dAMP kinase activity |
| A | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 195 |
| Chain | Residue |
| A | GLY16 |
| A | GLY18 |
| A | SER19 |
| A | GLY20 |
| A | LYS21 |
| A | GLY22 |
| A | ARG132 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 196 |
| Chain | Residue |
| A | LEU129 |
| A | ARG132 |
| A | ARG138 |
| A | ARG149 |
| A | LYS63 |
| A | GLN65 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FLIDGYPRevkQ |
| Chain | Residue | Details |
| A | PHE90-GLN101 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 29 |
| Details | Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2832612","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4367210","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2832612","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4367210","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2869483","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4366177","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00568","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1zio |
| Chain | Residue | Details |
| A | ARG138 | |
| A | LYS21 | |
| A | ASP140 | |
| A | ARG149 | |
| A | ASP141 | |
| A | ARG132 |






