2JED
The crystal structure of the kinase domain of the protein kinase C theta in complex with NVP-XAA228 at 2.32A resolution.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004697 | molecular_function | diacylglycerol-dependent serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004697 | molecular_function | diacylglycerol-dependent 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 | 15 |
| Details | BINDING SITE FOR RESIDUE LG8 A1701 |
| Chain | Residue |
| A | LEU386 |
| A | LEU461 |
| A | ASP465 |
| A | ASP508 |
| A | ASP522 |
| A | PHE664 |
| A | HOH2195 |
| A | GLY387 |
| A | PHE391 |
| A | VAL394 |
| A | ALA407 |
| A | GLU428 |
| A | THR442 |
| A | GLU459 |
| A | TYR460 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE LG8 B1712 |
| Chain | Residue |
| B | LEU386 |
| B | GLY387 |
| B | PHE391 |
| B | VAL394 |
| B | ALA407 |
| B | GLU428 |
| B | THR442 |
| B | MET458 |
| B | GLU459 |
| B | TYR460 |
| B | LEU461 |
| B | ASP465 |
| B | ASP508 |
| B | LEU511 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD B1713 |
| Chain | Residue |
| A | PHE597 |
| B | MET467 |
| B | ILE470 |
| B | GLU571 |
| B | GLY575 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGSFGKVFlAefkktnqf..........FAIK |
| Chain | Residue | Details |
| A | LEU386-LYS409 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvYrDLKldNILL |
| Chain | Residue | Details |
| A | ILE500-LEU512 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 508 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| 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 | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"11772397","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15364937","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16252004","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"11772397","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16252004","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2007","submissionDatabase":"PDB data bank","title":"The crystal structure of the kinase domain of the protein kinase C theta in complex with Nvp-Xaa228.","authors":["Stark W.","Bitsch F.","Berner A.","Buelens F.","Graff P.","Depersin H.","Fendrich G.","Geiser M.","Knecht R.","Rahuel J.","Rummel G.","Schlaeppi J.M.","Schmitz R.","Strauss A.","Wagner J."]}},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"11772397","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15364937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16252004","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2007","submissionDatabase":"PDB data bank","title":"The crystal structure of the kinase domain of the protein kinase C theta in complex with Nvp-Xaa228.","authors":["Stark W.","Bitsch F.","Berner A.","Buelens F.","Graff P.","Depersin H.","Fendrich G.","Geiser M.","Knecht R.","Rahuel J.","Rummel G.","Schlaeppi J.M.","Schmitz R.","Strauss A.","Wagner J."]}},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP504 | |
| A | ASP508 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP504 | |
| B | ASP508 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP504 | |
| A | LYS506 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP504 | |
| B | LYS506 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP504 | |
| A | THR542 | |
| A | LYS506 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP504 | |
| B | THR542 | |
| B | LYS506 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP504 | |
| A | LYS506 | |
| A | ASN509 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP504 | |
| B | LYS506 | |
| B | ASN509 |
