1IA9
CRYSTAL STRUCTURE OF THE ATYPICAL PROTEIN KINASE DOMAIN OF A TRP CA-CHANNEL, CHAK (AMPPNP COMPLEX)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 2001 |
| Chain | Residue |
| A | HIS1751 |
| A | HIS1808 |
| A | CYS1810 |
| A | CYS1814 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 2001 |
| Chain | Residue |
| B | HIS1751 |
| B | HIS1808 |
| B | CYS1810 |
| B | CYS1814 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ANP A 2002 |
| Chain | Residue |
| A | GLY1619 |
| A | GLY1620 |
| A | LEU1621 |
| A | ARG1622 |
| A | ALA1624 |
| A | LYS1646 |
| A | GLU1718 |
| A | GLU1719 |
| A | MET1721 |
| A | GLN1767 |
| A | ASP1775 |
| A | HOH3097 |
| A | HOH3191 |
| A | HOH3197 |
| B | THR1739 |
| A | MET1617 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DTT B 2000 |
| Chain | Residue |
| A | PRO1575 |
| A | GLU1578 |
| A | PRO1579 |
| B | CYS1606 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ANP B 2003 |
| Chain | Residue |
| B | MET1617 |
| B | GLY1620 |
| B | LEU1621 |
| B | ARG1622 |
| B | ALA1624 |
| B | LYS1646 |
| B | LEU1701 |
| B | GLU1718 |
| B | GLU1719 |
| B | MET1721 |
| B | PHE1725 |
| B | GLN1767 |
| B | ASP1775 |
| B | HOH3036 |
| B | HOH3037 |
| B | HOH3086 |
| B | HOH3110 |
| B | HOH3112 |
| B | HOH3130 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11389851","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IAH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11389851","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IA9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IAH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IAJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q96QT4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22222377","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 7 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q96QT4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 230 |
| Details | Domain: {"description":"Alpha-type protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00501","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
