2WTJ

CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR

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	13
Details	BINDING SITE FOR RESIDUE WTJ A 1513

Chain	Residue
A	LEU226
A	NO31515
A	HOH2066
A	HOH2132
A	HOH2246
A	ALA247
A	GLU302
A	LEU303
A	MET304
A	GLU305
A	GLU351
A	LEU354
A	ASP368

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NO3 A 1514

Chain	Residue
A	LEU375
A	GLY403
A	TYR404
A	ASN405
A	ARG406

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NO3 A 1515

Chain	Residue
A	LYS224
A	LYS245
A	LEU303
A	WTJ1513

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 1516

Chain	Residue
A	GLU219
A	ASN290
A	PHE291

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1517

Chain	Residue
A	LYS278
A	ILE288
A	LYS289
A	ASN290

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 1518

Chain	Residue
A	ALA215
A	PHE292

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 1519

Chain	Residue
A	ASN269
A	ARG346
A	HIS371
A	SER379
A	ARG382
A	THR383
A	HOH2102
A	HOH2248

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE343-LEU355

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP347

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
A	ILE448
A	ASP470
A	ARG523
A	GLU351
A	ASP368

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PLK3 => ECO:0000269|PubMed:16481012

Chain	Residue	Details
A	PRO283
A	ALA294

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by ATM and MAP3K20 => ECO:0000269|PubMed:10973490, ECO:0000269|PubMed:15342622, ECO:0000269|PubMed:16311512, ECO:0000269|PubMed:16481012

Chain	Residue	Details
A	LYS289

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18644861

Chain	Residue	Details
A	SER379

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:11390408

Chain	Residue	Details
A	THR383
A	THR387

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:17715138

Chain	Residue	Details
A	SER456

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP347
A	GLU351

---

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

Chain	Residue	Details
A	ASP347
A	LYS349

---

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

Chain	Residue	Details
A	ASP347
A	LYS349
A	THR387

---

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

Chain	Residue	Details
A	ASP347
A	ASN352
A	LYS349

---