5VT1

Crystal Structure of the Human CAMKK2B bound to a thiadiazinone benzamide 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	13
Details	binding site for residue 9JS A 501

Chain	Residue
A	ILE171
A	HOH609
A	HOH685
A	HOH705
A	HOH707
A	VAL179
A	ALA192
A	LYS194
A	LEU269
A	VAL270
A	GLN272
A	SER367
A	HOH604

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site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 502

Chain	Residue
A	HOH602
A	HOH608
A	HOH618
A	HOH631
A	HOH677
A	HOH679

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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. IGKGSYGVVKlAynendnty..........YAMK

Chain	Residue	Details
A	ILE171-LYS194

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

Chain	Residue	Details
A	ILE308-VAL320

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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	ASP312

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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	ILE171
A	LYS194

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