6S1F

Structure of the kinase domain of human RIPK2 in complex with the inhibitor CSLP3

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
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue KRE A 400

Chain	Residue
A	LEU24
A	ARG109
A	LEU153
A	ALA163
A	ASP164
A	SER29
A	VAL32
A	ALA45
A	LYS47
A	THR95
A	GLU96
A	MET98
A	GLU105

---

site_id	AC2
Number of Residues	15
Details	binding site for residue KRE B 400

Chain	Residue
B	LEU24
B	VAL32
B	ALA45
B	LYS47
B	LEU79
B	THR95
B	GLU96
B	TYR97
B	MET98
B	GLY101
B	GLU105
B	ASN151
B	LEU153
B	ALA163
B	ASP164

---

site_id	AC3
Number of Residues	12
Details	binding site for residue KRE C 400

Chain	Residue
C	LEU24
C	VAL32
C	ALA45
C	LYS47
C	THR95
C	GLU96
C	MET98
C	GLU105
C	ASN151
C	LEU153
C	ALA163
C	ASP164

---

site_id	AC4
Number of Residues	13
Details	binding site for residue KRE D 400

Chain	Residue
D	LEU24
D	VAL32
D	ALA45
D	LYS47
D	LEU79
D	THR95
D	GLU96
D	TYR97
D	MET98
D	GLY101
D	GLU105
D	ASN151
D	ASP164

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU142-LEU154

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:9705938

Chain	Residue	Details
A	ASP146
B	ASP146
C	ASP146
D	ASP146

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU24
B	LEU24
C	LEU24
D	LEU24

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	LYS47
B	LYS47
C	LYS47
D	LYS47

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: (Microbial infection) O-acetylthreonine; by Yersinia YopJ => ECO:0000269|PubMed:22520462

Chain	Residue	Details
A	THR149
A	THR189
B	THR149
B	THR189
C	THR149
C	THR189
D	THR149
D	THR189

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER168
B	SER168
C	SER168
D	SER168

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: Phosphoserine; alternate => ECO:0000269|PubMed:28545134

Chain	Residue	Details
A	SER174
D	SER174
D	SER178
D	SER181
A	SER178
A	SER181
B	SER174
B	SER178
B	SER181
C	SER174
C	SER178
C	SER181

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine; by autocatalysis and LRRK2; alternate => ECO:0000269|PubMed:16824733, ECO:0000269|PubMed:27830463, ECO:0000269|PubMed:28545134

Chain	Residue	Details
A	SER176
B	SER176
C	SER176
D	SER176

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:28545134

Chain	Residue	Details
A	SER180
B	SER180
C	SER180
D	SER180

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: (Microbial infection) O-acetylserine; by Yersinia YopJ => ECO:0000269|PubMed:22520462

Chain	Residue	Details
A	SER183
B	SER183
C	SER183
D	SER183

---

site_id	SWS_FT_FI10
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18079694

Chain	Residue	Details
A	LYS209
B	LYS209
C	LYS209
D	LYS209

---