5WNF

X-RAY CO-STRUCTURE OF RHO-ASSOCIATED PROTEIN KINASE (ROCK1) WITH A HIGHLY SELECTIVE 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue B4V A 501

Chain	Residue
A	ILE82
A	ASP117
A	PHE120
A	VAL137
A	GLU154
A	TYR155
A	MET156
A	LEU205
A	GLY218
A	PHE368
A	GLY85
A	ALA86
A	PHE87
A	GLY88
A	GLU89
A	VAL90
A	ALA103
A	LEU107

---

site_id	AC2
Number of Residues	5
Details	binding site for residue GOL A 502

Chain	Residue
A	ASP169
A	VAL170
A	MET271
A	LEU272
A	ASP304

---

site_id	AC3
Number of Residues	5
Details	binding site for residue GOL A 503

Chain	Residue
A	ASN163
A	SER166
A	ASN167
A	ASP369
C	GLU12

---

site_id	AC4
Number of Residues	17
Details	binding site for residue B4V B 900

Chain	Residue
B	GLY85
B	ALA86
B	PHE87
B	GLY88
B	GLU89
B	VAL90
B	ALA103
B	LEU107
B	ASP117
B	PHE120
B	VAL137
B	MET153
B	GLU154
B	TYR155
B	MET156
B	LEU205
B	GLY218

---

site_id	AC5
Number of Residues	19
Details	binding site for residue B4V C 900

Chain	Residue
C	ILE82
C	GLY85
C	ALA86
C	PHE87
C	GLY88
C	VAL90
C	ALA103
C	LEU107
C	ASP117
C	PHE120
C	VAL137
C	MET153
C	GLU154
C	TYR155
C	MET156
C	LEU205
C	ASP216
C	PHE368
C	HOH1009

---

site_id	AC6
Number of Residues	18
Details	binding site for residue B4V D 900

Chain	Residue
A	ASP281
D	ILE82
D	GLY85
D	ALA86
D	PHE87
D	VAL90
D	ALA103
D	ASP117
D	PHE120
D	VAL137
D	GLU154
D	TYR155
D	MET156
D	LEU205
D	PHE368
D	HOH1011
D	HOH1021
D	HOH1028

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE82-LYS105

---

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

Chain	Residue	Details
A	PHE194-LEU206

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	524
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	4
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	36
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---