2OWB

Structure of the Catalytic Domain of Human Polo-like Kinase 1

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	4
Details	BINDING SITE FOR RESIDUE ZN A 501

Chain	Residue
A	HIS93
A	CYS212
A	CYS255
A	ACT502

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT A 502

Chain	Residue
A	ZN501
A	HIS93
A	GLN94
A	LYS97
A	CYS212
A	LEU256

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT A 503

Chain	Residue
A	LYS178
A	LEU179
A	GLY180
A	ASN216
A	TYR217
A	HOH624
A	HOH674

---

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 626 A 500

Chain	Residue
A	ARG57
A	PHE58
A	LEU59
A	GLY62
A	ALA65
A	LYS66
A	CYS67
A	ALA80
A	LYS82
A	GLU131
A	CYS133
A	ARG134
A	ARG136
A	PHE183
A	HOH514
A	HOH538
A	HOH545

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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. LGKGGFAKCFeIsdadtkev..........FAGK

Chain	Residue	Details
A	LEU59-LYS82

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

Chain	Residue	Details
A	VAL172-LEU184

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:18615013

Chain	Residue	Details
A	ASP176

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
A	LYS82
A	GLU131
A	LYS178
A	ASP194
A	LEU59

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976

Chain	Residue	Details
A	SER103

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000305|PubMed:12207013

Chain	Residue	Details
A	SER137

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by AURKA => ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18615013, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	VAL210

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	THR214

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250

Chain	Residue	Details
A	SER269

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:12442251

Chain	Residue	Details
A	SER335

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site_id	SWS_FT_FI9
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18662541

Chain	Residue	Details
A	LYS19

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site_id	SWS_FT_FI10
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS338

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