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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6IL3

Crystal structure of the FLT3 kinase bound to a small molecule inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0004714	molecular_function	transmembrane receptor protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue A9R A 1001

Chain	Residue
A	LEU616
A	LEU818
A	ASP829
A	PHE830
A	ALA642
A	LYS644
A	VAL675
A	GLU692
A	TYR693
A	CYS694
A	GLY697
A	ASP698

site_id	AC2
Number of Residues	5
Details	binding site for residue PO4 A 1002

Chain	Residue
A	GLN580
A	ARG704
A	ASN841
A	ASN887
A	HOH1104

site_id	AC3
Number of Residues	9
Details	binding site for residue PO4 A 1003

Chain	Residue
A	GLU604
A	PHE605
A	PRO606
A	ARG607
A	THR682
A	LEU683
A	SER684
A	GLY846
A	HOH1118

site_id	AC4
Number of Residues	3
Details	binding site for residue PO4 A 1004

Chain	Residue
A	TYR696
A	HIS821
A	GLY822

site_id	AC5
Number of Residues	5
Details	binding site for residue PO4 A 1005

Chain	Residue
A	PHE570
A	ASN609
A	ALA620
A	ASP835
A	ARG849

site_id	AC6
Number of Residues	10
Details	binding site for residue CXS A 1006

Chain	Residue
A	GLN580
A	VAL592
A	TYR597
A	ARG704
A	ARG707
A	GLY885
A	VAL886
A	ASN887
A	GOL1011
A	HOH1106

site_id	AC7
Number of Residues	4
Details	binding site for residue CXS A 1007

Chain	Residue
A	LYS602
A	TRP603
A	GLU604
A	LEU678

site_id	AC8
Number of Residues	1
Details	binding site for residue GOL A 1008

Chain	Residue
A	HIS821

site_id	AC9
Number of Residues	5
Details	binding site for residue GOL A 1009

Chain	Residue
A	LYS907
A	PHE928
A	ASP929
A	LYS932
A	HOH1101

site_id	AD1
Number of Residues	2
Details	binding site for residue GOL A 1010

Chain	Residue
A	GLN910
A	GLU916

site_id	AD2
Number of Residues	6
Details	binding site for residue GOL A 1011

Chain	Residue
A	TYR597
A	ASN887
A	PRO890
A	GLY891
A	ILE892
A	CXS1006

site_id	AD3
Number of Residues	2
Details	binding site for residue GOL A 1012

Chain	Residue
A	ASP586
A	ARG931

site_id	AD4
Number of Residues	2
Details	binding site for residue GOL A 1013

Chain	Residue
A	ASN587
A	TYR589

site_id	AD5
Number of Residues	2
Details	binding site for residue GOL A 1014

Chain	Residue
A	PHE785
A	PHE912

site_id	AD6
Number of Residues	3
Details	binding site for residue GOL A 1015

Chain	Residue
A	SER584
A	SER585
A	GLU588

site_id	AD7
Number of Residues	3
Details	binding site for residue GOL A 1016

Chain	Residue
A	LYS623
A	LYS647
A	GLU648

site_id	AD8
Number of Residues	4
Details	binding site for residue GOL A 1017

Chain	Residue
A	TYR696
A	TYR702
A	SER705
A	LYS706

site_id	AD9
Number of Residues	6
Details	binding site for residue CL A 1018

Chain	Residue
A	GLN575
A	ASP811
A	ASN816
A	ASP829
A	PHE830
A	GLY831

site_id	AE1
Number of Residues	2
Details	binding site for residue CL A 1019

Chain	Residue
A	ASP835
A	HOH1123

site_id	AE2
Number of Residues	2
Details	binding site for residue CL A 1020

Chain	Residue
A	ARG834
A	ASP839

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	29
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGKVMnAtaygisktgvsiq.....VAVK

Chain	Residue	Details
A	LEU616-LYS644

site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CVHrDLAARNVLV

Chain	Residue	Details
A	CYS807-VAL819

site_id	PS00240
Number of Residues	14
Details	RECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GsHeNIVNLLGACT

Chain	Residue	Details
A	GLY669-THR682

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP811

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU616

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LYS644

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:16684964, ECO:0000269\|PubMed:21262971

Chain	Residue	Details
A	TYR572

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:16684964

Chain	Residue	Details
A	SER574

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:16684964, ECO:0000269\|PubMed:19477218, ECO:0000269\|PubMed:21262971

Chain	Residue	Details
A	TYR589
A	TYR599

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:15831474, ECO:0000269\|PubMed:16627759, ECO:0000269\|PubMed:16684964, ECO:0000269\|PubMed:19477218, ECO:0000269\|PubMed:21262971

Chain	Residue	Details
A	TYR591

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:16627759, ECO:0000269\|PubMed:19477218

Chain	Residue	Details
A	GLU777

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19369195

Chain	Residue	Details
A	ARG810

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:19477218, ECO:0000269\|PubMed:21262971

Chain	Residue	Details
A	TYR768
A	TYR793

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269\|PubMed:16627759, ECO:0000269\|PubMed:19477218, ECO:0000269\|PubMed:21262971

Chain	Residue	Details
A	TYR842
A	TYR955

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PDB entries from 2024-07-10

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