5LVL

Human PDK1 Kinase Domain in Complex with Compound PS653 Bound to the ATP-Binding Site

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine 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	8
Details	binding site for residue 537 A 401

Chain	Residue
A	LEU88
A	ALA109
A	LEU159
A	SER160
A	TYR161
A	ALA162
A	GLY165
A	LEU212

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site_id	AC2
Number of Residues	8
Details	binding site for residue DTD A 402

Chain	Residue
A	VAL243
A	GLY244
A	THR245
A	ALA246
A	GLU287
A	PHE291
A	HOH629
A	PHE242

---

site_id	AC3
Number of Residues	11
Details	binding site for residue DMS A 403

Chain	Residue
A	THR104
A	SER105
A	HIS139
A	PHE141
A	SER191
A	TRP347
A	GLU348
A	ASN349
A	LEU350
A	HIS351
A	HOH542

---

site_id	AC4
Number of Residues	5
Details	binding site for residue DMS A 404

Chain	Residue
A	PHE84
A	ILE112
A	LYS154
A	TYR156
A	GLU331

---

site_id	AC5
Number of Residues	4
Details	binding site for residue DMS A 405

Chain	Residue
A	TYR299
A	ASP300
A	PHE301
A	GLU314

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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. LGEGSFSTVVlArelatsre..........YAIK

Chain	Residue	Details
A	LEU88-LYS111

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

Chain	Residue	Details
A	ILE201-LEU213

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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	ASP205

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883

Chain	Residue	Details
A	SER92
A	LYS111
A	SER160
A	GLU166
A	ASP223

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:22999883

Chain	Residue	Details
A	GLU209

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:10455013, ECO:0000269|PubMed:11481331, ECO:0000269|PubMed:15772071, ECO:0000269|PubMed:16780920, ECO:0000269|Ref.8

Chain	Residue	Details
A	SEP241

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0

Chain	Residue	Details
A	LYS304

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756

Chain	Residue	Details
A	THR354

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