4HW7

Crystal structure of FMS kinase domain with a small molecular inhibitor, PLX647-OME

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	14
Details	BINDING SITE FOR RESIDUE 64M A 1001

Chain	Residue
A	ALA614
A	LEU785
A	ILE794
A	GLY795
A	ASP796
A	PHE797
A	LYS616
A	GLU633
A	LEU640
A	VAL647
A	THR663
A	GLU664
A	TYR665
A	CYS666

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Functional Information from PROSITE/UniProt

site_id	PS00024
Number of Residues	16
Details	HEMOPEXIN Hemopexin domain signature. LPvkWmapEsIFDSVY

Chain	Residue	Details
A	LEU817-TYR832

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

Chain	Residue	Details
A	LEU588-LYS616

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

Chain	Residue	Details
A	CYS774-LEU786

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

Chain	Residue	Details
A	GLY641-THR654

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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	PRO824

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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	LEU588

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

Chain	Residue	Details
A	LYS616

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20489731

Chain	Residue	Details
A	TYR546
A	ASP754
A	LEU769
A	PRO855

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:P09581

Chain	Residue	Details
A	TYR561

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20489731, ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	GLU745

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER759

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