3ZH8
A novel small molecule aPKC 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 |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IOD A 904 |
| Chain | Residue |
| A | LYS274 |
| A | PHE297 |
| A | ASP387 |
| A | TYR388 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 912 |
| Chain | Residue |
| A | ILE470 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE C58 A 1582 |
| Chain | Residue |
| A | ASP330 |
| A | ASP373 |
| A | LEU376 |
| A | THR386 |
| A | ASP387 |
| A | HOH2013 |
| A | ILE251 |
| A | VAL259 |
| A | GLU324 |
| A | VAL326 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1583 |
| Chain | Residue |
| A | GLY422 |
| A | PHE423 |
| A | SER424 |
| A | PRO492 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1584 |
| Chain | Residue |
| A | MET335 |
| A | ARG339 |
| A | GLU436 |
| A | GLY440 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 1585 |
| Chain | Residue |
| A | SER239 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IOD C 904 |
| Chain | Residue |
| C | LYS274 |
| C | PHE297 |
| C | ASP387 |
| C | TYR388 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 912 |
| Chain | Residue |
| C | HOH2017 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE C58 C 1580 |
| Chain | Residue |
| C | ILE251 |
| C | TYR256 |
| C | VAL259 |
| C | GLU324 |
| C | VAL326 |
| C | GLY329 |
| C | ASP330 |
| C | ASP373 |
| C | LEU376 |
| C | THR386 |
| C | ASP387 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 1581 |
| Chain | Residue |
| C | LYS371 |
| C | LEU372 |
| C | ASP373 |
| C | TYR410 |
| C | GLU436 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 1582 |
| Chain | Residue |
| C | CYS405 |
| C | GLY406 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 1583 |
| Chain | Residue |
| C | HIS303 |
| C | TYR359 |
| C | GLU362 |
| C | GLU522 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD B 901 |
| Chain | Residue |
| B | ASP558 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IOD B 904 |
| Chain | Residue |
| B | LYS274 |
| B | ASP387 |
| B | TYR388 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 912 |
| Chain | Residue |
| B | ILE470 |
| site_id | BC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE C58 B 1581 |
| Chain | Residue |
| B | ILE251 |
| B | GLY252 |
| B | VAL259 |
| B | GLU324 |
| B | VAL326 |
| B | ASP330 |
| B | ASP373 |
| B | LEU376 |
| B | THR386 |
| B | ASP387 |
| B | HOH2016 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1582 |
| Chain | Residue |
| B | GLY422 |
| B | PHE423 |
| B | SER424 |
| B | PRO492 |
| B | CYS498 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1583 |
| Chain | Residue |
| B | TYR256 |
| B | LYS371 |
| B | ASN374 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1584 |
| Chain | Residue |
| B | MET335 |
| B | GLU436 |
| B | GLY440 |
| B | ARG441 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1585 |
| Chain | Residue |
| B | ASN358 |
| B | HIS361 |
| B | PHE423 |
| B | TRP427 |
| B | GLY497 |
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 | ILE251-LYS278 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKldNVLL |
| Chain | Residue | Details |
| A | ILE365-LEU377 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| 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 | 27 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| 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 | 6 |
| 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 | 3 |
| 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 | 3 |
| 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 | ASP369 | proton shuttle (general acid/base) |
| A | LYS371 | electrostatic stabiliser |
| A | ASN374 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 756 |
| Chain | Residue | Details |
| B | ASP369 | proton shuttle (general acid/base) |
| B | LYS371 | electrostatic stabiliser |
| B | ASN374 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 756 |
| Chain | Residue | Details |
| C | ASP369 | proton shuttle (general acid/base) |
| C | LYS371 | electrostatic stabiliser |
| C | ASN374 | electrostatic stabiliser |
