5LI1
Structure of a Par3-inhibitory peptide bound to PKCiota core kinase domain
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue ANP A 601 |
| Chain | Residue |
| A | GLY261 |
| A | GLU333 |
| A | VAL335 |
| A | ASP339 |
| A | ASP382 |
| A | ASN383 |
| A | LEU385 |
| A | ASP396 |
| A | PHE552 |
| A | MG604 |
| A | HOH716 |
| A | GLY263 |
| A | HOH725 |
| A | HOH733 |
| A | HOH746 |
| A | HOH774 |
| A | SER264 |
| A | TYR265 |
| A | ALA266 |
| A | VAL268 |
| A | ALA281 |
| A | LYS283 |
| A | ILE332 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 602 |
| Chain | Residue |
| A | THR301 |
| A | ARG377 |
| A | CYS400 |
| A | LYS401 |
| A | GLU402 |
| A | TPO412 |
| A | HOH702 |
| A | HOH814 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue K A 603 |
| Chain | Residue |
| A | ALA309 |
| A | HIS312 |
| A | LEU315 |
| A | GLU333 |
| A | HOH815 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 604 |
| Chain | Residue |
| A | ASN383 |
| A | ASP396 |
| A | ANP601 |
| A | HOH774 |
| A | HOH781 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 605 |
| Chain | Residue |
| A | ASP292 |
| A | GLU294 |
| A | ASP295 |
| B | LYS16 |
| B | THR18 |
| B | HOH113 |
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 | 1 |
| 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 | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| 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 | 2 |
| 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 | 1 |
| 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 | 1 |
| 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 |
