2UV2

Crystal Structure Of Human Ste20-Like Kinase Bound To 4-(4-(5- Cyclopropyl-1H-pyrazol-3-ylamino)-quinazolin-2-ylamino)-phenyl)- acetonitrile

Replaces:  2JA0

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	3
Details	BINDING SITE FOR RESIDUE SCN A 1314

Chain	Residue
A	ARG242
A	LEU245
A	LYS249

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SCN A 1315

Chain	Residue
A	LYS63
A	VAL92
A	ILE108
A	ASP173
A	GVD1316
A	HOH2024

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 1309

Chain	Residue
A	HIS147
A	PRO211
A	TYR214
A	VAL218
A	THR282
A	THR283
A	EDO1311
A	HOH2144

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1310

Chain	Residue
A	VAL134
A	LYS137
A	GLN138
A	VAL294
A	ASP295
A	SER296
A	ASN297

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1311

Chain	Residue
A	HIS147
A	LYS150
A	ASP209
A	EDO1309

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 1312

Chain	Residue
A	ASN90
A	ASP168
A	HOH2055

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 1313

Chain	Residue
A	ASP27
A	GLN133
A	PRO290

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GVD A 1316

Chain	Residue
A	LEU40
A	ALA61
A	GLU109
A	CYS111
A	ALA112
A	LEU162
A	SCN1315
A	HOH2148

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGDGAFGKVYkAqnketsvl..........AAAK

Chain	Residue	Details
A	LEU40-LYS63

---

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

Chain	Residue	Details
A	ILE151-PHE163

---

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	ASP155

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU40
A	LYS63

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR10

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O54988

Chain	Residue	Details
A	THR183

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER189

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP155
A	GLY159

---

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

Chain	Residue	Details
A	ASP155
A	LYS157

---

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

Chain	Residue	Details
A	ASP155
A	THR193
A	LYS157

---

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

Chain	Residue	Details
A	ASP155
A	ASN160
A	LYS157

---