4RT7
Crystal Structure of FLT3 with a small molecule inhibitor
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 | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE P30 A 1001 |
Chain | Residue |
A | LEU616 |
A | GLY697 |
A | LEU818 |
A | CYS828 |
A | ASP829 |
A | PHE830 |
A | HOH1101 |
A | ALA642 |
A | LYS644 |
A | GLU661 |
A | LEU668 |
A | PHE691 |
A | TYR693 |
A | CYS694 |
A | CYS695 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 29 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGKVMnAtaygisktgvsiq.....VAVK |
Chain | Residue | Details |
A | LEU616-LYS644 |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CVHrDLAARNVLV |
Chain | Residue | Details |
A | CYS807-VAL819 |
site_id | PS00240 |
Number of Residues | 14 |
Details | RECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GsHeNIVNLLGACT |
Chain | Residue | Details |
A | GLY669-THR682 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 |
Chain | Residue | Details |
A | ASP811 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU616 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | LYS644 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:16684964, ECO:0000269|PubMed:21262971 |
Chain | Residue | Details |
A | TYR572 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:16684964 |
Chain | Residue | Details |
A | SER574 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16684964, ECO:0000269|PubMed:19477218, ECO:0000269|PubMed:21262971 |
Chain | Residue | Details |
A | TYR589 | |
A | TYR599 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15831474, ECO:0000269|PubMed:16627759, ECO:0000269|PubMed:16684964, ECO:0000269|PubMed:19477218, ECO:0000269|PubMed:21262971 |
Chain | Residue | Details |
A | TYR591 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16627759, ECO:0000269|PubMed:19477218 |
Chain | Residue | Details |
A | TYR726 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | SER759 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19477218, ECO:0000269|PubMed:21262971 |
Chain | Residue | Details |
A | TYR768 | |
A | TYR793 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16627759, ECO:0000269|PubMed:19477218, ECO:0000269|PubMed:21262971 |
Chain | Residue | Details |
A | TYR842 | |
A | TYR955 |