2JFL

CRYSTAL STRUCTURE OF HUMAN STE20-LIKE KINASE (DIPHOSPHORYLATED FORM) BOUND TO 5- AMINO-3-((4-(AMINOSULFONYL)PHENYL)AMINO)-N-(2,6- DIFLUOROPHENYL)-1H-1,2,4-TRIAZOLE-1-CARBOTHIOAMIDE

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	1
Details	BINDING SITE FOR RESIDUE SCN A 1315

Chain	Residue
A	ARG242

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 1316

Chain	Residue
A	DKI1309

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site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DKI A 1309

Chain	Residue
A	GLY114
A	GLY159
A	ASN160
A	LEU162
A	CL1316
A	HOH2145
A	LEU40
A	VAL48
A	ALA61
A	ILE108
A	GLU109
A	PHE110
A	CYS111

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1310

Chain	Residue
A	HIS147
A	PRO211
A	TYR214
A	THR282
A	THR283
A	EDO1312

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1311

Chain	Residue
A	VAL134
A	LYS137
A	GLN138
A	VAL294
A	SER296
A	ASN297
A	HOH2146

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1312

Chain	Residue
A	HIS147
A	LYS150
A	ASP209
A	EDO1310

---

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

Chain	Residue
A	PRO89
A	ASN90
A	HOH2048

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1314

Chain	Residue
A	ASP155
A	LYS157
A	ILE191
A	GLY192
A	THR193
A	PRO194

---

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

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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	TPO183

---

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	SEP189

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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

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