Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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

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

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
BTYR463
BTYR583
BTYR585
ATYR463
ATYR583
ATYR585

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
BTYR653
BTYR654
ATYR653
ATYR654

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

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon