2J51

Crystal structure of Human STE20-like kinase 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	2
Details	BINDING SITE FOR RESIDUE SCN A1313

Chain	Residue
A	ARG242
A	LYS249

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A1309

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

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A1310

Chain	Residue
A	VAL134
A	LYS137
A	GLN138
A	VAL294
A	SER296
A	ASN297
A	EDO1312

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A1311

Chain	Residue
A	HIS147
A	LYS150
A	ASP209
A	EDO1309

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A1312

Chain	Residue
A	ASN90
A	ASP168
A	EDO1310
A	HOH2050

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DKI A1314

Chain	Residue
A	LEU40
A	VAL48
A	ALA61
A	ILE108
A	GLU109
A	PHE110
A	CYS111
A	GLY114
A	GLY159
A	ASN160
A	LEU162
A	HOH2151

---

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	258
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"O54988","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

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

---