3C4E
Pim-1 Kinase Domain in Complex with 3-aminophenyl-7-azaindole
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 | 0043066 | biological_process | negative regulation of apoptotic process |
| 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 | 0043066 | biological_process | negative regulation of apoptotic process |
| 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 | 0043066 | biological_process | negative regulation of apoptotic process |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0043066 | biological_process | negative regulation of apoptotic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IMD A 1 |
| Chain | Residue |
| A | PHE130 |
| A | THR134 |
| A | ASP170 |
| A | ASP234 |
| A | GLY238 |
| A | ASP239 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE IMD B 2 |
| Chain | Residue |
| B | ASP170 |
| B | ASP234 |
| B | GLY238 |
| B | ASP239 |
| B | PHE130 |
| B | ILE133 |
| B | THR134 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IMD C 3 |
| Chain | Residue |
| C | PHE130 |
| C | THR134 |
| C | ASP170 |
| C | ASP234 |
| C | GLY238 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE IMD D 4 |
| Chain | Residue |
| D | PHE130 |
| D | ILE133 |
| D | THR134 |
| D | ASP170 |
| D | ASP234 |
| D | GLY238 |
| D | ASP239 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE C4E A 306 |
| Chain | Residue |
| A | PHE49 |
| A | ALA65 |
| A | LYS67 |
| A | ILE104 |
| A | GLU121 |
| A | ARG122 |
| A | LEU174 |
| A | ASP186 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE C4E B 306 |
| Chain | Residue |
| B | PHE49 |
| B | ALA65 |
| B | LYS67 |
| B | GLU121 |
| B | ARG122 |
| B | LEU174 |
| B | ILE185 |
| B | ASP186 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE C4E C 306 |
| Chain | Residue |
| C | LEU44 |
| C | PHE49 |
| C | ALA65 |
| C | LYS67 |
| C | GLU121 |
| C | ARG122 |
| C | LEU174 |
| C | ILE185 |
| C | ASP186 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE C4E D 306 |
| Chain | Residue |
| D | LEU44 |
| D | PHE49 |
| D | ALA65 |
| D | LYS67 |
| D | ILE104 |
| D | GLU121 |
| D | ARG122 |
| D | LEU174 |
| D | ILE185 |
| D | ASP186 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK |
| Chain | Residue | Details |
| A | LEU44-LYS67 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI |
| Chain | Residue | Details |
| A | VAL163-ILE175 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1008 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15525646","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15657054","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15808862","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15657054","evidenceCode":"ECO:0000269"}]} |
| 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 | ASP167 | |
| A | GLU171 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR204 | |
| B | LYS169 | |
| B | ASP167 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | THR204 | |
| C | LYS169 | |
| C | ASP167 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | THR204 | |
| D | LYS169 | |
| D | ASP167 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN172 | |
| A | LYS169 | |
| A | ASP167 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN172 | |
| B | LYS169 | |
| B | ASP167 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASN172 | |
| C | LYS169 | |
| C | ASP167 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASN172 | |
| D | LYS169 | |
| D | ASP167 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP167 | |
| B | GLU171 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP167 | |
| C | GLU171 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP167 | |
| D | GLU171 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS169 | |
| A | ASP167 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS169 | |
| B | ASP167 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | LYS169 | |
| C | ASP167 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | LYS169 | |
| D | ASP167 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR204 | |
| A | LYS169 | |
| A | ASP167 |
