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6P68

Crystal structure of FGFR1-Y563C (FGFR4 surrogate) covalently bound to compound 22.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005007molecular_functionfibroblast growth factor receptor activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005007molecular_functionfibroblast growth factor receptor activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005007molecular_functionfibroblast growth factor receptor activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue O1Y A 801
ChainResidue
ALEU484
AGLU571
ALEU630
AALA640
AASP641
APHE642
ALEU494
AALA512
ALYS514
AGLU531
AMET535
AGLU562
ACYS563
AALA564

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 802
ChainResidue
AARG470
ATRP471
ALEU548
AGLY549

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 B 802
ChainResidue
BARG470
BTRP471
BGLU472
BLEU548

site_idAC4
Number of Residues15
Detailsbinding site for Di-peptide O1Y B 801 and CYS B 563
ChainResidue
BLEU484
BVAL492
BLEU494
BLYS510
BALA512
BLYS514
BGLU531
BMET535
BILE545
BVAL561
BGLU562
BALA564
BSER565
BALA640
BASP641

site_idAC5
Number of Residues16
Detailsbinding site for Di-peptide O1Y C 801 and CYS C 563
ChainResidue
CLEU484
CVAL492
CLEU494
CLYS510
CALA512
CLYS514
CGLU531
CMET535
CILE545
CVAL561
CGLU562
CALA564
CSER565
CLEU630
CALA640
CASP641

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVlAeaigldkdkpnrvtk...VAVK
ChainResidueDetails
ALEU484-LYS514

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV
ChainResidueDetails
ACYS619-VAL631

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19224897
ChainResidueDetails
AASP623
BASP623
CASP623

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING:
ChainResidueDetails
ALEU484
BASN568
BARG627
BASP641
CLEU484
CLYS514
CGLU562
CASN568
CARG627
CASP641
ALYS514
AGLU562
AASN568
AARG627
AASP641
BLEU484
BLYS514
BGLU562

site_idSWS_FT_FI3
Number of Residues9
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701
ChainResidueDetails
ATYR463
ATYR583
ATYR585
BTYR463
BTYR583
BTYR585
CTYR463
CTYR583
CTYR585

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701
ChainResidueDetails
ATYR653
ATYR654
BTYR653
BTYR654
CTYR653
CTYR654

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701
ChainResidueDetails
ATYR730
BTYR730
CTYR730

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PDB entries from 2024-03-27

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