1RJB

Crystal Structure of FLT3

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 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

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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

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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

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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	GLU862

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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

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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

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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

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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

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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	VAL819
A	VAL844

---

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	PRO893

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ARG815
A	ASP811

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ALA813
A	ASP811

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site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ALA813
A	ASN816
A	ASP811

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