Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5W5O

Identification of potent and selective RIPK2 inhibitors for the treatment of inflammatory diseases.

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
E	0004672	molecular_function	protein kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004672	molecular_function	protein kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0004672	molecular_function	protein kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
H	0004672	molecular_function	protein kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation
I	0004672	molecular_function	protein kinase activity
I	0005524	molecular_function	ATP binding
I	0006468	biological_process	protein phosphorylation
J	0004672	molecular_function	protein kinase activity
J	0005524	molecular_function	ATP binding
J	0006468	biological_process	protein phosphorylation
K	0004672	molecular_function	protein kinase activity
K	0005524	molecular_function	ATP binding
K	0006468	biological_process	protein phosphorylation
L	0004672	molecular_function	protein kinase activity
L	0005524	molecular_function	ATP binding
L	0006468	biological_process	protein phosphorylation
M	0004672	molecular_function	protein kinase activity
M	0005524	molecular_function	ATP binding
M	0006468	biological_process	protein phosphorylation
N	0004672	molecular_function	protein kinase activity
N	0005524	molecular_function	ATP binding
N	0006468	biological_process	protein phosphorylation
O	0004672	molecular_function	protein kinase activity
O	0005524	molecular_function	ATP binding
O	0006468	biological_process	protein phosphorylation
P	0004672	molecular_function	protein kinase activity
P	0005524	molecular_function	ATP binding
P	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue 9XA A 401

Chain	Residue
A	LEU24
A	GLU105
A	LEU153
A	ASP164
A	SER25
A	VAL32
A	ALA45
A	LEU79
A	THR95
A	GLU96
A	TYR97
A	MET98

site_id	AC2
Number of Residues	18
Details	binding site for residue 9XA B 401

Chain	Residue
B	LEU24
B	SER25
B	VAL32
B	ALA45
B	LEU79
B	ILE93
B	THR95
B	GLU96
B	TYR97
B	MET98
B	PRO99
B	GLY101
B	SER102
B	GLU105
B	ARG109
B	LEU153
B	ALA163
B	ASP164

site_id	AC3
Number of Residues	14
Details	binding site for residue 9XA C 401

Chain	Residue
C	LEU24
C	SER25
C	VAL32
C	ALA45
C	LYS47
C	GLU96
C	TYR97
C	MET98
C	PRO99
C	GLY101
C	SER102
C	LEU153
C	ALA163
C	ASP164

site_id	AC4
Number of Residues	11
Details	binding site for residue 9XA D 401

Chain	Residue
D	LEU24
D	SER25
D	VAL32
D	ALA45
D	LEU79
D	THR95
D	GLU96
D	TYR97
D	MET98
D	LEU153
D	ASP164

site_id	AC5
Number of Residues	12
Details	binding site for residue 9XA E 401

Chain	Residue
E	LEU24
E	SER25
E	VAL32
E	ALA45
E	LEU79
E	THR95
E	GLU96
E	TYR97
E	MET98
E	GLU105
E	LEU153
E	ASP164

site_id	AC6
Number of Residues	15
Details	binding site for residue 9XA F 401

Chain	Residue
F	LEU24
F	SER25
F	VAL32
F	ALA45
F	LEU79
F	THR95
F	GLU96
F	TYR97
F	MET98
F	PRO99
F	GLU105
F	ARG109
F	LEU153
F	ASP164
F	HOH503

site_id	AC7
Number of Residues	12
Details	binding site for residue 9XA G 401

Chain	Residue
G	LEU24
G	SER25
G	VAL32
G	ALA45
G	LEU79
G	THR95
G	GLU96
G	TYR97
G	MET98
G	GLU105
G	LEU153
G	ASP164

site_id	AC8
Number of Residues	13
Details	binding site for residue 9XA H 401

Chain	Residue
H	THR95
H	GLU96
H	TYR97
H	MET98
H	GLY101
H	GLU105
H	LEU153
H	ASP164
H	LEU24
H	SER25
H	VAL32
H	ALA45
H	LEU79

site_id	AC9
Number of Residues	12
Details	binding site for residue 9XA I 401

Chain	Residue
I	LEU24
I	SER25
I	VAL32
I	ALA45
I	LEU79
I	THR95
I	GLU96
I	TYR97
I	MET98
I	GLY101
I	LEU153
I	ASP164

site_id	AD1
Number of Residues	14
Details	binding site for residue 9XA J 401

Chain	Residue
J	LEU24
J	SER25
J	VAL32
J	ALA45
J	LEU79
J	THR95
J	GLU96
J	TYR97
J	MET98
J	PRO99
J	GLU105
J	GLN150
J	LEU153
J	ASP164

site_id	AD2
Number of Residues	13
Details	binding site for residue 9XA K 401

Chain	Residue
K	LEU24
K	SER25
K	VAL32
K	ALA45
K	LEU79
K	THR95
K	GLU96
K	TYR97
K	MET98
K	GLY101
K	GLU105
K	LEU153
K	ASP164

site_id	AD3
Number of Residues	14
Details	binding site for residue 9XA L 401

Chain	Residue
L	LEU24
L	SER25
L	VAL32
L	ALA45
L	LYS47
L	LEU79
L	THR95
L	GLU96
L	TYR97
L	MET98
L	GLY101
L	GLU105
L	LEU153
L	ASP164

site_id	AD4
Number of Residues	12
Details	binding site for residue 9XA M 401

Chain	Residue
M	LEU24
M	SER25
M	VAL32
M	ALA45
M	LEU79
M	THR95
M	GLU96
M	TYR97
M	MET98
M	GLU105
M	LEU153
M	ASP164

site_id	AD5
Number of Residues	12
Details	binding site for residue 9XA N 401

Chain	Residue
N	LEU24
N	SER25
N	VAL32
N	ALA45
N	LEU79
N	THR95
N	GLU96
N	TYR97
N	MET98
N	GLY101
N	LEU153
N	ASP164

site_id	AD6
Number of Residues	14
Details	binding site for residue 9XA O 401

Chain	Residue
O	LEU24
O	SER25
O	VAL32
O	ALA45
O	LEU79
O	ILE93
O	THR95
O	GLU96
O	TYR97
O	MET98
O	PRO99
O	GLU105
O	LEU153
O	ASP164

site_id	AD7
Number of Residues	16
Details	binding site for residue 9XA P 401

Chain	Residue
P	ARG22
P	LEU24
P	SER25
P	VAL32
P	ALA45
P	LYS47
P	LEU79
P	ILE93
P	THR95
P	GLU96
P	MET98
P	GLY101
P	SER102
P	LEU153
P	ALA163
P	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	16
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:9705938

Chain	Residue	Details
A	ASP146
J	ASP146
K	ASP146
L	ASP146
M	ASP146
N	ASP146
O	ASP146
P	ASP146
B	ASP146
C	ASP146
D	ASP146
E	ASP146
F	ASP146
G	ASP146
H	ASP146
I	ASP146

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU24
J	LEU24
K	LEU24
L	LEU24
M	LEU24
N	LEU24
O	LEU24
P	LEU24
B	LEU24
C	LEU24
D	LEU24
E	LEU24
F	LEU24
G	LEU24
H	LEU24
I	LEU24

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING:

Chain	Residue	Details
A	LYS47
J	LYS47
K	LYS47
L	LYS47
M	LYS47
N	LYS47
O	LYS47
P	LYS47
B	LYS47
C	LYS47
D	LYS47
E	LYS47
F	LYS47
G	LYS47
H	LYS47
I	LYS47

site_id	SWS_FT_FI4
Number of Residues	32
Details	MOD_RES: (Microbial infection) O-acetylthreonine; by Yersinia YopJ => ECO:0000269\|PubMed:22520462

Chain	Residue	Details
A	THR149
E	THR189
F	THR149
F	THR189
G	THR149
G	THR189
H	THR149
H	THR189
I	THR149
I	THR189
J	THR149
A	THR189
J	THR189
K	THR149
K	THR189
L	THR149
L	THR189
M	THR149
M	THR189
N	THR149
N	THR189
O	THR149
B	THR149
O	THR189
P	THR149
P	THR189
B	THR189
C	THR149
C	THR189
D	THR149
D	THR189
E	THR149

site_id	SWS_FT_FI5
Number of Residues	16
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19369195

Chain	Residue	Details
A	SER168
J	SER168
K	SER168
L	SER168
M	SER168
N	SER168
O	SER168
P	SER168
B	SER168
C	SER168
D	SER168
E	SER168
F	SER168
G	SER168
H	SER168
I	SER168

site_id	SWS_FT_FI6
Number of Residues	48
Details	MOD_RES: Phosphoserine; alternate => ECO:0000269\|PubMed:28545134

Chain	Residue	Details
A	SER174
D	SER174
D	SER178
D	SER181
E	SER174
E	SER178
E	SER181
F	SER174
F	SER178
F	SER181
G	SER174
A	SER178
G	SER178
G	SER181
H	SER174
H	SER178
H	SER181
I	SER174
I	SER178
I	SER181
J	SER174
J	SER178
A	SER181
J	SER181
K	SER174
K	SER178
K	SER181
L	SER174
L	SER178
L	SER181
M	SER174
M	SER178
M	SER181
B	SER174
N	SER174
N	SER178
N	SER181
O	SER174
O	SER178
O	SER181
P	SER174
P	SER178
P	SER181
B	SER178
B	SER181
C	SER174
C	SER178
C	SER181

site_id	SWS_FT_FI7
Number of Residues	16
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
J	SER176
K	SER176
L	SER176
M	SER176
N	SER176
O	SER176
P	SER176
B	SER176
C	SER176
D	SER176
E	SER176
F	SER176
G	SER176
H	SER176
I	SER176

site_id	SWS_FT_FI8
Number of Residues	16
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:28545134

Chain	Residue	Details
A	SER180
J	SER180
K	SER180
L	SER180
M	SER180
N	SER180
O	SER180
P	SER180
B	SER180
C	SER180
D	SER180
E	SER180
F	SER180
G	SER180
H	SER180
I	SER180

site_id	SWS_FT_FI9
Number of Residues	16
Details	MOD_RES: (Microbial infection) O-acetylserine; by Yersinia YopJ => ECO:0000269\|PubMed:22520462

Chain	Residue	Details
A	SER183
J	SER183
K	SER183
L	SER183
M	SER183
N	SER183
O	SER183
P	SER183
B	SER183
C	SER183
D	SER183
E	SER183
F	SER183
G	SER183
H	SER183
I	SER183

site_id	SWS_FT_FI10
Number of Residues	32
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:18079694

Chain	Residue	Details
A	LYS209
F	LYS209
G	LYS209
H	LYS209
I	LYS209
J	LYS209
K	LYS209
L	LYS209
M	LYS209
N	LYS209
O	LYS209
B	LYS209
P	LYS209
C	LYS209
D	LYS209
E	LYS209

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)