5VJA
Crystal Structure of human zipper-interacting protein kinase (ZIPK, alias DAPK3) in complex with a pyrazolo[3,4-d]pyrimidinone ligand (HS38)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 1001 |
| Chain | Residue |
| A | ILE177 |
| A | PHE178 |
| A | PRO181 |
| A | LEU226 |
| A | HOH1122 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue DUK A 1002 |
| Chain | Residue |
| A | LEU93 |
| A | VAL96 |
| A | MET146 |
| A | ILE160 |
| A | ASP161 |
| A | HOH1109 |
| A | HOH1158 |
| A | HOH1161 |
| A | HOH1175 |
| A | LEU19 |
| A | GLY20 |
| A | VAL27 |
| A | LYS42 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 1001 |
| Chain | Residue |
| B | ILE177 |
| B | PHE178 |
| B | GLY179 |
| B | PRO181 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue DUK B 1002 |
| Chain | Residue |
| B | LEU19 |
| B | VAL27 |
| B | LYS42 |
| B | LEU93 |
| B | VAL96 |
| B | ASP161 |
| B | HOH1110 |
| B | HOH1132 |
| B | HOH1148 |
| B | HOH1233 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 1001 |
| Chain | Residue |
| C | ILE177 |
| C | GLY179 |
| C | HOH1191 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue DUK C 1002 |
| Chain | Residue |
| C | LEU19 |
| C | GLY22 |
| C | LYS42 |
| C | LEU93 |
| C | MET146 |
| C | ILE160 |
| C | ASP161 |
| C | HOH1117 |
| C | HOH1136 |
| C | HOH1163 |
| C | HOH1192 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue ILE D 301 |
| Chain | Residue |
| D | ILE275 |
| D | LYS276 |
| D | ALA277 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue DMS D 302 |
| Chain | Residue |
| D | PHE178 |
| D | GLY179 |
| D | HOH492 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue DUK D 303 |
| Chain | Residue |
| D | LEU19 |
| D | GLY22 |
| D | VAL27 |
| D | LYS42 |
| D | LEU93 |
| D | MET146 |
| D | ILE160 |
| D | ASP161 |
| D | HOH429 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 28 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAIVRkCrqkgtgkeyaak......FIKK |
| Chain | Residue | Details |
| A | LEU19-LYS46 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHfDLKpeNIML |
| Chain | Residue | Details |
| A | ILE135-LEU147 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 172 |
| Details | Region: {"description":"Activation segment","evidences":[{"source":"UniProtKB","id":"O96017","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18239682","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J90","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"15611134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17158456","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"15611134","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis and ROCK1","evidences":[{"source":"PubMed","id":"15611134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17158456","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18239682","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18239682","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
