2J7T

Crystal structure of human serine threonine kinase-10 bound to SU11274

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	5
Details	BINDING SITE FOR RESIDUE CA A 332

Chain	Residue
A	HOH2013
A	HOH2014
A	HOH2016
A	HOH2019
A	HOH2058

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 333

Chain	Residue
A	HOH2130
A	HOH2020
A	HOH2051
A	HOH2059
A	HOH2129

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A1318

Chain	Residue
A	GLU168
A	GLU316
A	HOH2054
A	HOH2125
A	HOH2127
A	HOH2128

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A1319

Chain	Residue
A	GLU313
A	GLU316
A	HOH2055
A	HOH2128

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A1320

Chain	Residue
A	GLU234
A	HOH2078
A	HOH2079
A	HOH2080

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA A1321

Chain	Residue
A	GLN135
A	HOH2039
A	HOH2108

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A1322

Chain	Residue
A	GLU124
A	GLU313
A	HOH2028
A	HOH2126

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT A1323

Chain	Residue
A	THR298
A	VAL314

---

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 274 A1324

Chain	Residue
A	LEU42
A	ALA63
A	GLU81
A	ILE108
A	ILE110
A	GLU111
A	PHE112
A	CYS113
A	GLY116
A	ALA117
A	LEU164
A	ASP175
A	HOH2007
A	HOH2129

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU42-LYS65

---

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

Chain	Residue	Details
A	ILE153-MET165

---

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	ASP157

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU42

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LYS65

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:E9PTG8

Chain	Residue	Details
A	SER20

---

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

Chain	Residue	Details
A	SER191

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLY161
A	ASP157

---

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

Chain	Residue	Details
A	ASP157
A	LYS159

---

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

Chain	Residue	Details
A	THR195
A	ASP157
A	LYS159

---

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

Chain	Residue	Details
A	ASP157
A	ASN162
A	LYS159

---