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4F63

Crystal structure of Human Fibroblast Growth Factor Receptor 1 Kinase domain in complex with compound 1

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 0S7 A 801
ChainResidue
ALEU484
AGLY567
AASP641
AHOH918
AGLY485
AVAL492
AALA512
AVAL561
AGLU562
ATYR563
AALA564
ASER565

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 802
ChainResidue
AGLU531
AMET535
AASP641
AGLY643

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 803
ChainResidue
ATRP684
ATYR701
AARG718
AMET719
ATRP737
AHOH917

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 0S7 B 801
ChainResidue
BLEU484
BALA512
BVAL561
BGLU562
BTYR563
BALA564
BSER565
BGLY567
BARG627
BASN628
BLEU630
BALA640
BASP641

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 802
ChainResidue
BGLU531
BASP641
BPHE642
BGLY643

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 803
ChainResidue
BTRP684
BTYR701
BLEU713
BHIS717
BARG718
BMET719
BTRP737

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

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PDB entries from 2024-04-24

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