5VC4

Crystal structure of HUMAN WEE1 KINASE domain in complex with Bosutinib-isomer

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 XZN A 601

Chain	Residue
A	GLU303
A	CYS379
A	GLY382
A	PHE433
A	ASP463
A	HOH744
A	ILE305
A	ALA326
A	LYS328
A	VAL360
A	ILE374
A	ASN376
A	GLU377
A	TYR378

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site_id	AC2
Number of Residues	5
Details	binding site for residue PO4 A 602

Chain	Residue
A	HIS494
A	PRO496
A	LYS497
A	HOH702
A	HOH723

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGEFGSVFkCvkrldgci..........YAIK

Chain	Residue	Details
A	ILE305-LYS328

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

Chain	Residue	Details
A	LEU422-ILE434

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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:PRU10027

Chain	Residue	Details
A	ASP426

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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	ILE305
A	LYS328

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15837193

Chain	Residue	Details
A	ASN342
A	ASN431
A	ASP463
A	GLY465

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER307

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER312

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