2ZM1

Crystal structure of imidazo pyrazin 1 bound to the kinase domain of human LCK, (auto-phosphorylated on TYR394)

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 SO4 A 510

Chain	Residue
A	GLN298
A	ARG299
A	SER377
A	LYS379
A	TYR457
A	ARG458
A	ARG474
A	HOH518

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 511

Chain	Residue
A	GLY266
A	HIS267
A	TYR489
A	TYR263

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMS A 512

Chain	Residue
A	TRP233
A	GLU239
A	THR308
A	GLN309
A	HOH740
A	HOH746

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site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE KSF A 513

Chain	Residue
A	LEU251
A	ALA271
A	LYS273
A	GLU288
A	THR316
A	GLU317
A	TYR318
A	MET319
A	LEU371
A	HOH679

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	23
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGQFGEVWmGyynghtk...........VAVK

Chain	Residue	Details
A	LEU251-LYS273

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

Chain	Residue	Details
A	TYR360-VAL372

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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	ASP364

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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	LEU251
A	LYS273

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8139546

Chain	Residue	Details
A	PTR394

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by CSK => ECO:0000269|PubMed:1639064, ECO:0000269|PubMed:8139546, ECO:0000269|PubMed:8631775, ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692

Chain	Residue	Details
A	TYR505

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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	ALA368
A	ASP364

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

Chain	Residue	Details
A	ASP364
A	ARG366

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

Chain	Residue	Details
A	ASP364
A	ARG366
A	ASN369

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