6JQR

Crystal structure of FLT3 in complex with gilteritinib

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	10
Details	binding site for residue C6F A 1001

Chain	Residue
A	LEU616
A	PHE830
A	ALA642
A	GLU692
A	TYR693
A	CYS694
A	CYS695
A	GLY697
A	ASP698
A	LEU818

---

site_id	AC2
Number of Residues	9
Details	binding site for residue SO4 A 1002

Chain	Residue
A	GLU604
A	PHE605
A	ARG607
A	CYS681
A	THR682
A	LEU683
A	SER684
A	VAL844
A	GLY846

---

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 1003

Chain	Residue
A	GLN580
A	ARG704
A	ASN841
A	HOH1139

---

site_id	AC4
Number of Residues	3
Details	binding site for residue SO4 A 1004

Chain	Residue
A	TYR696
A	HIS821
A	GLY822

---

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL A 1006

Chain	Residue
A	LYS907
A	ALA927
A	PHE928
A	ASP929
A	LYS932

---

site_id	AC6
Number of Residues	9
Details	binding site for residue CXS A 1007

Chain	Residue
A	GLN580
A	PHE590
A	VAL592
A	TYR597
A	ARG704
A	ARG707
A	GLY885
A	VAL886
A	ASN887

---

site_id	AC7
Number of Residues	8
Details	binding site for residue GOL A 1008

Chain	Residue
A	PRO893
A	ASN897
A	HOH1102
A	HOH1102
A	HOH1103
A	HOH1103
A	HOH1106
A	HOH1106

---

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	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16627759, ECO:0000269|PubMed:19477218, ECO:0000269|PubMed:21262971

Chain	Residue	Details
A	TYR842

---