8H75
FGFR2 in complex with YJ001
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 |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004713 | molecular_function | protein tyrosine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004672 | molecular_function | protein kinase activity |
D | 0004713 | molecular_function | protein tyrosine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 31 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGCFGQVVmAeavgidkdkpkeavt...VAVK |
Chain | Residue | Details |
A | LEU487-LYS517 |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV |
Chain | Residue | Details |
A | CYS622-VAL634 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 80 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | GLY490-GLU510 | |
B | GLY490-GLU510 | |
C | GLY490-GLU510 | |
D | GLY490-GLU510 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19060208 |
Chain | Residue | Details |
A | ASP738 | |
B | ASP738 | |
C | ASP738 | |
D | ASP738 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 |
Chain | Residue | Details |
A | THR599 | |
C | ALA629 | |
C | ASP677 | |
C | GLN683 | |
D | THR599 | |
D | ALA629 | |
D | ASP677 | |
D | GLN683 | |
A | ALA629 | |
A | ASP677 | |
A | GLN683 | |
B | THR599 | |
B | ALA629 | |
B | ASP677 | |
B | GLN683 | |
C | THR599 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 |
Chain | Residue | Details |
A | ALA578 | |
A | GLY700 | |
B | ALA578 | |
B | GLY700 | |
C | ALA578 | |
C | GLY700 | |
D | ALA578 | |
D | GLY700 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 |
Chain | Residue | Details |
A | THR698 | |
A | GLU768 | |
B | THR698 | |
B | GLU768 | |
C | THR698 | |
C | GLU768 | |
D | THR698 | |
D | GLU768 |