6ILZ
Crystal structure of PKCiota in complex with inhibitor
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 | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007163 | biological_process | establishment or maintenance of cell polarity |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0007163 | biological_process | establishment or maintenance of cell polarity |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0004674 | molecular_function | protein serine/threonine kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
| E | 0007163 | biological_process | establishment or maintenance of cell polarity |
| G | 0004672 | molecular_function | protein kinase activity |
| G | 0004674 | molecular_function | protein serine/threonine kinase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006468 | biological_process | protein phosphorylation |
| G | 0007163 | biological_process | establishment or maintenance of cell polarity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue AFU A 601 |
| Chain | Residue |
| A | ILE260 |
| A | LYS283 |
| A | GLU333 |
| A | TYR334 |
| A | VAL335 |
| A | THR395 |
| A | ASP396 |
| A | PHE552 |
| A | ASP553 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue AFU C 601 |
| Chain | Residue |
| C | ILE260 |
| C | VAL316 |
| C | ILE332 |
| C | GLU333 |
| C | TYR334 |
| C | VAL335 |
| C | THR395 |
| C | ASP396 |
| C | PHE552 |
| C | ASP553 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue AFU E 601 |
| Chain | Residue |
| E | ILE260 |
| E | ILE332 |
| E | GLU333 |
| E | TYR334 |
| E | VAL335 |
| E | LEU385 |
| E | THR395 |
| E | ASP396 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue AFU G 601 |
| Chain | Residue |
| G | ILE260 |
| G | VAL268 |
| G | ILE332 |
| G | GLU333 |
| G | VAL335 |
| G | THR395 |
| G | ASP396 |
| G | PHE552 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 28 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGSYAKVLlVrlkktdriyamk......VVKK |
| Chain | Residue | Details |
| A | ILE260-LYS287 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKldNVLL |
| Chain | Residue | Details |
| A | ILE374-LEU386 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| 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_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"11713277","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11891849","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"11713277","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"16125198","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"16125198","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 756 |
| Chain | Residue | Details |
| A | ASP378 | proton shuttle (general acid/base) |
| A | LYS380 | electrostatic stabiliser |
| A | ASN383 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 756 |
| Chain | Residue | Details |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 756 |
| Chain | Residue | Details |
| C | ASP378 | proton shuttle (general acid/base) |
| C | LYS380 | electrostatic stabiliser |
| C | ASN383 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 756 |
| Chain | Residue | Details |
