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3RHX

Crystal structure of the catalytic domain of FGFR1 kinase in complex with ARQ 069

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 Residues10
DetailsBINDING SITE FOR RESIDUE 3RH B 1
ChainResidue
BHOH93
BASP641
BALA512
BGLU531
BILE545
BVAL561
BGLU562
BTYR563
BALA564
BLEU630

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 766
ChainResidue
BHOH84
BARG570
BARG627
BTHR657
BASN659
BARG661

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 767
ChainResidue
APRO741
BHOH4
BHOH457
BGLU462

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 3RH A 2
ChainResidue
AVAL492
AALA512
AGLU531
AVAL561
AGLU562
AALA564
ALEU630
AALA640
AASP641

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1
ChainResidue
AHOH15
AHOH368
AARG470
AGLU533
ALYS536
AMET537
ALYS618

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 766
ChainResidue
AGLU752
AASP753
AARG756

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 767
ChainResidue
AHOH53
AHOH186
ATRP691
ASER699
APRO702
AHOH797
BASP720

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 768
ChainResidue
AHOH3
ATRP684
ATYR701
AARG718
AMET719
ATRP737

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVlAeaigldkdkpnrvtk...VAVK
ChainResidueDetails
BLEU484-LYS514

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV
ChainResidueDetails
BCYS619-VAL631

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16507368","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16507368","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19665973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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