7JNT

CRYSTAL STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE 2 (ROCK2) IN COMPLEX WITH A POTENT AND SELECTIVE DUAL ROCK INHIBITOR

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
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
E	0004672	molecular_function	protein kinase activity
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004672	molecular_function	protein kinase activity
F	0004674	molecular_function	protein serine/threonine kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0004672	molecular_function	protein kinase activity
G	0004674	molecular_function	protein serine/threonine kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
H	0004672	molecular_function	protein kinase activity
H	0004674	molecular_function	protein serine/threonine kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue VFA A 501

Chain	Residue
A	ILE98
A	VAL153
A	MET169
A	GLU170
A	TYR171
A	MET172
A	LEU221
A	ASP232
A	PHE384
A	MES502
A	GLY101
A	ALA102
A	PHE103
A	GLY104
A	VAL106
A	ALA119
A	LYS121
A	LEU123

---

site_id	AC2
Number of Residues	8
Details	binding site for residue MES A 502

Chain	Residue
A	PHE103
A	ASP133
A	PHE136
A	ARG213
A	GLY234
A	THR235
A	MET237
A	VFA501

---

site_id	AC3
Number of Residues	16
Details	binding site for residue VFA B 501

Chain	Residue
B	ILE98
B	GLY101
B	PHE103
B	GLY104
B	GLU105
B	ALA119
B	LYS121
B	LEU123
B	MET169
B	GLU170
B	TYR171
B	MET172
B	LEU221
B	ALA231
B	ASP232
B	PHE384

---

site_id	AC4
Number of Residues	2
Details	binding site for residue CL B 502

Chain	Residue
B	PHE354
B	TRP361

---

site_id	AC5
Number of Residues	19
Details	binding site for residue VFA C 501

Chain	Residue
C	ILE98
C	GLY101
C	PHE103
C	GLY104
C	GLU105
C	VAL106
C	ALA119
C	LYS121
C	LEU123
C	MET169
C	GLU170
C	TYR171
C	MET172
C	LEU221
C	ALA231
C	ASP232
C	PHE384
C	HOH634
C	HOH646

---

site_id	AC6
Number of Residues	1
Details	binding site for residue CL C 502

Chain	Residue
C	PHE354

---

site_id	AC7
Number of Residues	19
Details	binding site for residue VFA D 501

Chain	Residue
D	ILE98
D	GLY101
D	ALA102
D	PHE103
D	GLY104
D	GLU105
D	VAL106
D	ALA119
D	LYS121
D	LEU123
D	VAL153
D	MET169
D	GLU170
D	TYR171
D	MET172
D	LEU221
D	ASP232
D	PHE384
D	MES502

---

site_id	AC8
Number of Residues	6
Details	binding site for residue MES D 502

Chain	Residue
D	PHE103
D	ASP133
D	PHE136
D	ARG213
D	GLY234
D	VFA501

---

site_id	AC9
Number of Residues	17
Details	binding site for residue VFA E 501

Chain	Residue
E	TYR171
E	MET172
E	LEU221
E	ASP232
E	PHE384
E	MES502
E	HOH631
E	ILE98
E	GLY101
E	PHE103
E	GLY104
E	VAL106
E	ALA119
E	LYS121
E	LEU123
E	MET169
E	GLU170

---

site_id	AD1
Number of Residues	6
Details	binding site for residue MES E 502

Chain	Residue
E	PHE103
E	ASP133
E	PHE136
E	ARG213
E	GLY234
E	VFA501

---

site_id	AD2
Number of Residues	18
Details	binding site for residue VFA F 501

Chain	Residue
F	ILE98
F	GLY101
F	PHE103
F	GLY104
F	GLU105
F	VAL106
F	ALA119
F	LYS121
F	LEU123
F	MET169
F	GLU170
F	TYR171
F	MET172
F	LEU221
F	ALA231
F	ASP232
F	PHE384
F	MES503

---

site_id	AD3
Number of Residues	1
Details	binding site for residue CL F 502

Chain	Residue
F	PHE354

---

site_id	AD4
Number of Residues	7
Details	binding site for residue MES F 503

Chain	Residue
F	PHE103
F	ASP133
F	PHE136
F	ARG213
F	GLY234
F	VAL251
F	VFA501

---

site_id	AD5
Number of Residues	16
Details	binding site for residue VFA G 501

Chain	Residue
G	ILE98
G	GLY101
G	PHE103
G	GLY104
G	VAL106
G	ALA119
G	LYS121
G	LEU123
G	MET169
G	GLU170
G	TYR171
G	MET172
G	LEU221
G	ASP232
G	PHE384
G	MES502

---

site_id	AD6
Number of Residues	6
Details	binding site for residue MES G 502

Chain	Residue
G	PHE103
G	ASP133
G	PHE136
G	ARG213
G	GLY234
G	VFA501

---

site_id	AD7
Number of Residues	20
Details	binding site for residue VFA H 501

Chain	Residue
H	ILE98
H	GLY101
H	ALA102
H	PHE103
H	GLY104
H	GLU105
H	VAL106
H	ALA119
H	LYS121
H	LEU123
H	MET169
H	GLU170
H	TYR171
H	MET172
H	LEU221
H	ALA231
H	ASP232
H	PHE384
H	MES502
H	HOH627

---

site_id	AD8
Number of Residues	10
Details	binding site for residue MES H 502

Chain	Residue
H	ASP133
H	PHE136
H	ARG213
H	GLY234
H	THR235
H	MET237
H	THR249
H	VAL251
H	VFA501
H	HOH615

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE98-LYS121

---

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

Chain	Residue	Details
A	LEU210-LEU222

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
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_FI2
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"Phosphothreonine; by ROCK2","evidences":[{"source":"UniProtKB","id":"Q62868","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---