5XFJ

Crystal structure of LY2874455 in complex of FGFR4 gatekeeper mutation (V550M)

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	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue 6LF A 801

Chain	Residue
A	LEU473
A	ASN557
A	ARG616
A	LEU619
A	GLU475
A	ALA501
A	LYS503
A	GLU551
A	CYS552
A	ALA553
A	ALA554
A	GLY556

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	31
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVrAeafgmdparpdqast...VAVK

Chain	Residue	Details
A	LEU473-LYS503

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

Chain	Residue	Details
A	CYS608-VAL620

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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	ASP612

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU473
A	LYS503

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER573

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:18670643

Chain	Residue	Details
A	TYR642
A	TYR643

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