6SK9

Nek2 bound to purine compound 51

Replaces:  6H0O

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 F9N A 301

Chain	Residue
A	GLY15
A	SER96
A	LYS100
A	GLU104
A	PHE148
A	HOH418
A	THR16
A	CYS22
A	LYS37
A	GLU87
A	TYR88
A	CYS89
A	GLY92
A	ASP93

---

site_id	AC2
Number of Residues	6
Details	binding site for residue GOL A 302

Chain	Residue
A	LEU122
A	ASP242
A	HIS276
A	HIS277
A	HOH411
A	HOH441

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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. VlHrDLKpaNVFL

Chain	Residue	Details
A	VAL137-LEU149

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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	ASP141

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE14

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	LYS37

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000305|PubMed:17197699

Chain	Residue	Details
A	THR170

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000305|PubMed:17197699, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER171

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17197699

Chain	Residue	Details
A	THR175
A	THR179

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER184

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:17197699

Chain	Residue	Details
A	SER241

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