2RKU

Structure of PLK1 in complex with BI2536

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	TLA502

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE R78 A 500

Chain	Residue
A	VAL114
A	LEU130
A	GLU131
A	LEU132
A	CYS133
A	ARG136
A	PHE183
A	HOH527
A	HOH563
A	HOH619
A	ARG57
A	PHE58
A	LEU59
A	LYS61
A	GLU69

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TLA A 502

Chain	Residue
A	LYS91
A	HIS93
A	LYS97
A	CYS212
A	SER254
A	CYS255
A	LEU256
A	ZN501
A	TLA504
A	HOH608
A	HOH677

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TLA A 504

Chain	Residue
A	PHE64
A	LYS91
A	GLN94
A	LYS97
A	TLA502
A	HOH552
A	HOH608
A	HOH733

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SRT A 505

Chain	Residue
A	ASN266
A	TYR268
A	SER269
A	ILE270
A	GLN283

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SRT A 507

Chain	Residue
A	ARG135
A	GLU140
A	LEU141
A	LEU319
A	HOH592
A	HOH648
A	HOH698

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TAR A 503

Chain	Residue
A	LEU139
A	LYS178
A	LEU179
A	GLY180
A	ASN216
A	HOH743
A	HOH783

---

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

---

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

---

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	LEU59
A	LYS82
A	GLU131
A	LYS178
A	ASP194

---

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

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	GLY180
A	ASP176

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS178
A	ASP176

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	THR214
A	LYS178
A	ASP176

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASN181
A	LYS178
A	ASP176

---