6BQQ

Crystal Structure of the Human CAMKK2B in complex with BI2526

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	11
Details	binding site for residue R78 A 501

Chain	Residue
A	ILE171
A	LYS338
A	HOH659
A	VAL179
A	VAL249
A	PHE267
A	GLU268
A	LEU269
A	VAL270
A	ASN271
A	LEU319

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site_id	AC2
Number of Residues	4
Details	binding site for residue ACT A 502

Chain	Residue
A	SER159
A	LYS168
A	ASP169
A	HOH644

---

site_id	AC3
Number of Residues	6
Details	binding site for residue ACT A 503

Chain	Residue
A	GLN272
A	ARG311
A	ASN335
A	LEU344
A	SER345
A	ASN346

---

site_id	AC4
Number of Residues	3
Details	binding site for residue ACT A 504

Chain	Residue
A	ASP169
A	TYR190
A	ILE365

---

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

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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