2YIT

Structural analysis of checkpoint kinase 2 in complex with PV1162, a novel inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein 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	14
Details	BINDING SITE FOR RESIDUE YIT A 600

Chain	Residue
A	LEU226
A	THR367
A	ASP368
A	GLY370
A	HOH2035
A	HOH2042
A	VAL234
A	ILE251
A	GLU273
A	LEU277
A	MET304
A	GLU305
A	GLY307
A	LEU354

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NO3 A 601

Chain	Residue
A	LEU375
A	GLY403
A	TYR404
A	ASN405
A	ARG406

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Functional Information from PROSITE/UniProt

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNVLL

Chain	Residue	Details
A	ILE343-LEU355

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP347

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
A	GLY227
A	LYS249
A	GLU302
A	GLU351
A	ASP368

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18644861

Chain	Residue	Details
A	SER379

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:11390408

Chain	Residue	Details
A	THR383
A	THR387

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:17715138

Chain	Residue	Details
A	SER456

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