2BWJ
Structure of adenylate kinase 5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004017 | molecular_function | AMP kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| A | 0046034 | biological_process | ATP metabolic process |
| B | 0004017 | molecular_function | AMP kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| B | 0046034 | biological_process | ATP metabolic process |
| C | 0004017 | molecular_function | AMP kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| C | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| C | 0046034 | biological_process | ATP metabolic process |
| D | 0004017 | molecular_function | AMP kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| D | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| D | 0046034 | biological_process | ATP metabolic process |
| E | 0004017 | molecular_function | AMP kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| E | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| E | 0046034 | biological_process | ATP metabolic process |
| F | 0004017 | molecular_function | AMP kinase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| F | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| F | 0046034 | biological_process | ATP metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 A1199 |
| Chain | Residue |
| A | GLY19 |
| A | HOH2123 |
| A | HOH2124 |
| A | GLY21 |
| A | SER22 |
| A | GLY23 |
| A | LYS24 |
| A | GLY25 |
| A | HOH2120 |
| A | HOH2121 |
| A | HOH2122 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A1200 |
| Chain | Residue |
| A | SER54 |
| A | GLU55 |
| A | HOH2125 |
| B | SER138 |
| B | LEU140 |
| B | HOH2080 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A1201 |
| Chain | Residue |
| A | ALA125 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 B1199 |
| Chain | Residue |
| B | GLY19 |
| B | PRO20 |
| B | GLY21 |
| B | SER22 |
| B | GLY23 |
| B | LYS24 |
| B | GLY25 |
| B | HOH2009 |
| B | HOH2099 |
| B | HOH2100 |
| B | HOH2101 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B1200 |
| Chain | Residue |
| A | HOH2042 |
| B | ARG152 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 C1198 |
| Chain | Residue |
| C | GLY19 |
| C | GLY21 |
| C | SER22 |
| C | GLY23 |
| C | LYS24 |
| C | GLY25 |
| C | HOH2003 |
| C | HOH2005 |
| C | HOH2084 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D1197 |
| Chain | Residue |
| D | GLY19 |
| D | GLY21 |
| D | SER22 |
| D | GLY23 |
| D | LYS24 |
| D | GLY25 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 E1198 |
| Chain | Residue |
| E | GLY19 |
| E | GLY21 |
| E | SER22 |
| E | GLY23 |
| E | LYS24 |
| E | GLY25 |
| E | HOH2039 |
| E | HOH2040 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL E1199 |
| Chain | Residue |
| E | ALA125 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 F1199 |
| Chain | Residue |
| F | GLY19 |
| F | GLY21 |
| F | SER22 |
| F | GLY23 |
| F | LYS24 |
| F | GLY25 |
| F | HOH2006 |
| F | HOH2010 |
| F | HOH2096 |
| F | HOH2097 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL F1200 |
| Chain | Residue |
| C | ARG66 |
| F | ARG100 |
| F | TYR156 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL F1201 |
| Chain | Residue |
| F | ARG158 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE AMP B1201 |
| Chain | Residue |
| B | GLU29 |
| B | HIS39 |
| B | HOH2102 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE AMP C1199 |
| Chain | Residue |
| C | HIS39 |
| C | HOH2086 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE AMP F1202 |
| Chain | Residue |
| F | GLU29 |
| F | HIS39 |
| F | HOH2098 |
| F | HOH2099 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FLIDGYPRevkQ |
| Chain | Residue | Details |
| A | PHE93-GLN104 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1092 |
| Details | Region: {"description":"Adenylate kinase 2","evidences":[{"source":"PubMed","id":"19647735","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 174 |
| Details | Region: {"description":"NMP 2","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of adenylate kinase 5.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 60 |
| Details | Region: {"description":"LID 2","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of adenylate kinase 5.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 96 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00568","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






