5FLF
DISEASE LINKED MUTATION IN FGFR
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 | 0005007 | molecular_function | fibroblast growth factor receptor 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 | 0005007 | molecular_function | fibroblast growth factor receptor 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 | 0005007 | molecular_function | fibroblast growth factor receptor 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 | 0005007 | molecular_function | fibroblast growth factor receptor activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0004713 | molecular_function | protein tyrosine kinase activity |
| E | 0005007 | molecular_function | fibroblast growth factor receptor activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 E 1762 |
| Chain | Residue |
| D | THR726 |
| D | ASN727 |
| D | GLU728 |
| D | HOH2085 |
| E | LYS617 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1764 |
| Chain | Residue |
| D | SER699 |
| D | HOH2088 |
| B | THR726 |
| B | ASN727 |
| D | ARG577 |
| D | GLY698 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1765 |
| Chain | Residue |
| D | ARG570 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1763 |
| Chain | Residue |
| A | ARG622 |
| A | ARG646 |
| A | TYR654 |
| A | ARG661 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1764 |
| Chain | Residue |
| C | ARG622 |
| C | ARG646 |
| C | TYR654 |
| C | LYS656 |
| C | THR657 |
| C | ARG661 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1765 |
| Chain | Residue |
| B | ARG622 |
| B | ARG646 |
| B | TYR654 |
| B | LYS656 |
| B | ARG661 |
| B | HOH2048 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1766 |
| Chain | Residue |
| D | LYS523 |
| D | ARG622 |
| D | LEU644 |
| D | ARG646 |
| D | TYR654 |
| D | LYS656 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1767 |
| Chain | Residue |
| D | ASP735 |
| D | HIS738 |
| D | GLN743 |
| E | LYS542 |
| E | TYR605 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1768 |
| Chain | Residue |
| D | LYS566 |
| D | ARG576 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PGE C 1765 |
| Chain | Residue |
| C | ALA615 |
| C | HIS679 |
| C | GLN680 |
| C | VAL683 |
| C | PRO741 |
| C | ARG744 |
| C | PRO745 |
| C | THR746 |
| C | PHE747 |
| C | LYS748 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PGE D 1769 |
| Chain | Residue |
| B | HIS649 |
| D | SER530 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE D 1770 |
| Chain | Residue |
| D | THR746 |
| D | PHE747 |
| D | LYS748 |
| D | GLN749 |
| D | CL1772 |
| D | HOH2045 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PGE D 1771 |
| Chain | Residue |
| D | ARG470 |
| D | TRP471 |
| D | GLU472 |
| D | LEU500 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 1766 |
| Chain | Residue |
| B | PHE747 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 1772 |
| Chain | Residue |
| D | PHE747 |
| D | PGE1770 |
| site_id | BC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL D 1773 |
| Chain | Residue |
| D | LYS514 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 1774 |
| Chain | Residue |
| D | TYR701 |
| D | HIS717 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 1764 |
| Chain | Residue |
| A | THR726 |
| A | ASN727 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 31 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVlAeaigldkdkpnrvtk...VAVK |
| Chain | Residue | Details |
| A | LEU484-LYS514 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV |
| Chain | Residue | Details |
| A | CYS619-VAL631 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19224897 |
| Chain | Residue | Details |
| A | ASP623 | |
| B | ASP623 | |
| C | ASP623 | |
| D | ASP623 | |
| E | ASP623 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU484 | |
| B | ASN568 | |
| B | ARG627 | |
| B | ASP641 | |
| C | LEU484 | |
| C | LYS514 | |
| C | GLU562 | |
| C | ASN568 | |
| C | ARG627 | |
| C | ASP641 | |
| D | LEU484 | |
| A | LYS514 | |
| D | LYS514 | |
| D | GLU562 | |
| D | ASN568 | |
| D | ARG627 | |
| D | ASP641 | |
| E | LEU484 | |
| E | LYS514 | |
| E | GLU562 | |
| E | ASN568 | |
| E | ARG627 | |
| A | GLU562 | |
| E | ASP641 | |
| A | ASN568 | |
| A | ARG627 | |
| A | ASP641 | |
| B | LEU484 | |
| B | LYS514 | |
| B | GLU562 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701 |
| Chain | Residue | Details |
| A | TYR463 | |
| D | TYR463 | |
| D | TYR583 | |
| D | TYR585 | |
| E | TYR463 | |
| E | TYR583 | |
| E | TYR585 | |
| A | TYR583 | |
| A | TYR585 | |
| B | TYR463 | |
| B | TYR583 | |
| B | TYR585 | |
| C | TYR463 | |
| C | TYR583 | |
| C | TYR585 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701 |
| Chain | Residue | Details |
| A | TYR653 | |
| E | TYR654 | |
| A | TYR654 | |
| B | TYR653 | |
| B | TYR654 | |
| C | TYR653 | |
| C | TYR654 | |
| D | TYR653 | |
| D | TYR654 | |
| E | TYR653 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701 |
| Chain | Residue | Details |
| A | TYR730 | |
| B | TYR730 | |
| C | TYR730 | |
| D | TYR730 | |
| E | TYR730 |
