7JOV

CRYSTAL STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE 2 (ROCK2) IN COMPLEX WITH A PHENYLPYRAZOLE AMIDE 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	5
Details	binding site for residue MES A 501

Chain	Residue
A	PHE103
A	ASP133
A	PHE136
A	ARG213
A	GLY234

---

site_id	AC2
Number of Residues	13
Details	binding site for residue VFS A 502

Chain	Residue
A	GLU105
A	VAL106
A	ALA119
A	LYS121
A	GLU170
A	TYR171
A	MET172
A	LEU221
A	ASP232
A	ILE98
A	ARG100
A	GLY101
A	GLY104

---

site_id	AC3
Number of Residues	14
Details	binding site for residue VFS B 501

Chain	Residue
B	ILE98
B	ARG100
B	GLY101
B	GLY104
B	GLU105
B	VAL106
B	ALA119
B	LYS121
B	MET169
B	GLU170
B	TYR171
B	MET172
B	LEU221
B	ASP232

---

site_id	AC4
Number of Residues	14
Details	binding site for residue VFS C 501

Chain	Residue
C	ILE98
C	GLY104
C	GLU105
C	VAL106
C	ALA119
C	LYS121
C	MET169
C	GLU170
C	TYR171
C	MET172
C	ASN219
C	LEU221
C	ASP232
C	PHE384

---

site_id	AC5
Number of Residues	1
Details	binding site for residue CL C 502

Chain	Residue
C	ASN356

---

site_id	AC6
Number of Residues	14
Details	binding site for residue VFS D 501

Chain	Residue
D	ILE98
D	GLY101
D	GLY104
D	GLU105
D	VAL106
D	ALA119
D	LYS121
D	LEU123
D	GLU170
D	TYR171
D	MET172
D	LEU221
D	ALA231
D	ASP232

---

site_id	AC7
Number of Residues	12
Details	binding site for residue VFS E 501

Chain	Residue
E	ILE98
E	ARG100
E	GLY101
E	GLU105
E	VAL106
E	ALA119
E	LYS121
E	GLU170
E	TYR171
E	MET172
E	LEU221
E	ASP232

---

site_id	AC8
Number of Residues	7
Details	binding site for residue MES F 501

Chain	Residue
F	PHE103
F	ASP133
F	PHE136
F	ARG213
F	GLY234
F	THR249
F	VAL251

---

site_id	AC9
Number of Residues	12
Details	binding site for residue VFS F 502

Chain	Residue
F	ILE98
F	GLY101
F	GLY104
F	GLU105
F	VAL106
F	ALA119
F	LYS121
F	GLU170
F	TYR171
F	MET172
F	LEU221
F	ASP232

---

site_id	AD1
Number of Residues	2
Details	binding site for residue CL F 503

Chain	Residue
F	PHE354
F	TRP361

---

site_id	AD2
Number of Residues	13
Details	binding site for residue VFS G 501

Chain	Residue
G	ALA119
G	LYS121
G	MET169
G	GLU170
G	TYR171
G	MET172
G	LEU221
G	ASP232
G	ILE98
G	ARG100
G	GLY101
G	GLU105
G	VAL106

---

site_id	AD3
Number of Residues	13
Details	binding site for residue VFS H 501

Chain	Residue
H	ILE98
H	GLY101
H	GLY104
H	GLU105
H	VAL106
H	ALA119
H	LYS121
H	MET169
H	GLU170
H	TYR171
H	MET172
H	LEU221
H	ASP232

---

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	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP214
B	ASP214
C	ASP214
D	ASP214
E	ASP214
F	ASP214
G	ASP214
H	ASP214

---

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

Chain	Residue	Details
A	ILE98
E	LYS121
F	ILE98
F	LYS121
G	ILE98
G	LYS121
H	ILE98
H	LYS121
A	LYS121
B	ILE98
B	LYS121
C	ILE98
C	LYS121
D	ILE98
D	LYS121
E	ILE98

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by ROCK2 => ECO:0000250|UniProtKB:Q62868

Chain	Residue	Details
A	THR414
B	THR414
C	THR414
D	THR414
E	THR414
F	THR414
G	THR414
H	THR414

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