4RX8

SYK Catalytic Domain Complexed with a Potent Triazine Inhibitor2

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	8
Details	BINDING SITE FOR RESIDUE GOL A 701

Chain	Residue
A	PHE382
A	LYS402
A	ASP494
A	ARG498
A	ASN499
A	ASP512
A	3YX703
A	HOH804

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 702

Chain	Residue
A	MET450
A	GLU452
A	ASN615
A	HOH837
A	HOH895
A	LYS387

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site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3YX A 703

Chain	Residue
A	LEU377
A	SER379
A	ALA400
A	MET448
A	GLU449
A	ALA451
A	GLU452
A	GLY454
A	PRO455
A	ARG498
A	ASN499
A	LEU501
A	SER511
A	ASP512
A	GOL701

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	26
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGNFGTVKkGyyqmkkvvkt........VAVK

Chain	Residue	Details
A	LEU377-LYS402

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

Chain	Residue	Details
A	PHE490-LEU502

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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	ASP494

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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	LEU377
A	LYS402

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site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:21469132

Chain	Residue	Details
A	TYR364
A	TYR484
A	TYR507
A	TYR526
A	TYR629
A	TYR631

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:21469132

Chain	Residue	Details
A	SER379
A	SER579

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site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:21469132

Chain	Residue	Details
A	THR384
A	THR530
A	THR582

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:21469132

Chain	Residue	Details
A	TYR525

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P48025

Chain	Residue	Details
A	TYR546

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:21469132

Chain	Residue	Details
A	TYR630

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