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1FGI

CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF FIBROBLAST GROWTH FACTOR RECEPTOR 1 IN COMPLEX WITH SU5402 INHIBITOR

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
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SU1 B 1000
ChainResidue
BHOH228
BGLY567
BASN568
BLEU630
BGLY485
BPHE489
BALA512
BILE545
BVAL561
BGLU562
BTYR563
BALA564

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SU1 A 1001
ChainResidue
AHOH229
AGLY485
APHE489
AALA512
AILE545
AVAL561
AGLU562
ATYR563
AALA564
AGLY567
AASN568
ALEU630

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19224897
ChainResidueDetails
AASP623
BASP623

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
ALEU484
BASN568
BARG627
BASP641
ALYS514
AGLU562
AASN568
AARG627
AASP641
BLEU484
BLYS514
BGLU562

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701
ChainResidueDetails
ATYR463
ATYR583
ATYR585
BTYR463
BTYR583
BTYR585

site_idSWS_FT_FI4
Number of Residues4
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

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701
ChainResidueDetails
ATYR730
BTYR730

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG627
AASP623

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG627
BASP623

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA625
AASP623

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA625
BASP623

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR658
AALA625
AASP623

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN628
AALA625
AASP623

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN628
BALA625
BASP623

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PDB entries from 2024-05-01

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