5HES
Human leucine zipper- and sterile alpha motif-containing kinase (ZAK, MLT, HCCS-4, MRK, AZK, MLTK) in complex with vemurafenib
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue 032 A 401 |
| Chain | Residue |
| A | GLY23 |
| A | TYR84 |
| A | ALA85 |
| A | ASP92 |
| A | CYS150 |
| A | ASP151 |
| A | PHE152 |
| A | GLY153 |
| A | HOH501 |
| A | HOH527 |
| A | PHE27 |
| A | VAL30 |
| A | ALA43 |
| A | LYS45 |
| A | ILE66 |
| A | ILE80 |
| A | THR82 |
| A | GLU83 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | ARG63 |
| A | ASP144 |
| A | LYS148 |
| B | PRO126 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue 032 B 401 |
| Chain | Residue |
| B | GLY23 |
| B | PHE27 |
| B | VAL30 |
| B | ALA43 |
| B | LYS45 |
| B | ILE66 |
| B | THR82 |
| B | GLU83 |
| B | TYR84 |
| B | ALA85 |
| B | ASP92 |
| B | CYS150 |
| B | ASP151 |
| B | PHE152 |
| B | GLY153 |
| B | HOH548 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| A | PRO126 |
| B | ASP144 |
| B | LYS148 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDLKsrNVVI |
| Chain | Residue | Details |
| A | VAL129-ILE141 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P80192","evidenceCode":"ECO:0000250"},{"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 | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P80192","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11836244","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"32289254","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"15342622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26999302","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"15342622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26999302","evidenceCode":"ECO:0000269"}]} |
| 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":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
