1U4D
Structure of the ACK1 Kinase Domain bound to Debromohymenialdisine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004713 | molecular_function | protein tyrosine 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 | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 502 |
| Chain | Residue |
| B | ARG251 |
| B | GLN287 |
| B | ARG290 |
| B | HOH533 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE DBQ A 398 |
| Chain | Residue |
| A | LEU207 |
| A | ALA208 |
| A | ASN257 |
| A | ASP270 |
| A | HOH415 |
| A | HOH440 |
| A | HOH450 |
| A | ASP134 |
| A | ALA156 |
| A | LYS158 |
| A | THR205 |
| A | GLU206 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DBQ B 401 |
| Chain | Residue |
| B | LEU132 |
| B | ALA156 |
| B | LYS158 |
| B | THR205 |
| B | GLU206 |
| B | LEU207 |
| B | ALA208 |
| B | ASN257 |
| B | LEU259 |
| B | ASP270 |
| B | HOH503 |
| B | HOH523 |
| B | HOH584 |
| B | HOH589 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 27 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGDGSFGVVRrGewdapsgktvs.......VAVK |
| Chain | Residue | Details |
| A | LEU132-LYS158 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNLLL |
| Chain | Residue | Details |
| A | PHE248-LEU260 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by SRC and autocatalysis","evidences":[{"source":"PubMed","id":"15308621","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16472662","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20333297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20623637","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20979614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21169560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21309750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19369195","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 | ARG256 | |
| A | ASP252 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ARG256 | |
| B | ASP252 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ALA254 | |
| A | ASP252 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ALA254 | |
| B | ASP252 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ALA254 | |
| A | ASN257 | |
| A | ASP252 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ALA254 | |
| B | ASN257 | |
| B | ASP252 |
