4TYJ

Structural analysis of the human Fibroblast Growth Factor Receptor 4 Kinase

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	17
Details	binding site for residue 0LI A 801

Chain	Residue
A	ALA501
A	CYS608
A	ILE609
A	HIS610
A	LEU619
A	ILE628
A	ALA629
A	ASP630
A	PHE631
A	LYS503
A	GLU520
A	MET524
A	ILE527
A	ILE533
A	VAL550
A	GLU551
A	ALA553

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site_id	AC2
Number of Residues	5
Details	binding site for residue EDO A 802

Chain	Residue
A	LYS531
A	ASN535
A	GLU551
A	LYS627
A	HOH956

---

site_id	AC3
Number of Residues	6
Details	binding site for residue PO4 A 803

Chain	Residue
A	GLU461
A	PHE462
A	ARG464
A	CYS540
A	GLN542
A	GLU543

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site_id	AC4
Number of Residues	6
Details	binding site for residue PO4 A 804

Chain	Residue
A	ARG707
A	ARG723
A	TRP726
A	HIS727
A	HOH923
A	HOH930

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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. LGEGCFGQVVrAeafgmdparpdqast...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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