Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5K0B

Crystal Structure of COMT in complex with 2,4-dimethyl-5-[3-(1-phenylethyl)-1H-pyrazol-5-yl]-1,3-thiazole

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0006584	biological_process	catecholamine metabolic process
A	0008171	molecular_function	O-methyltransferase activity
A	0016206	molecular_function	catechol O-methyltransferase activity
B	0000287	molecular_function	magnesium ion binding
B	0006584	biological_process	catecholamine metabolic process
B	0008171	molecular_function	O-methyltransferase activity
B	0016206	molecular_function	catechol O-methyltransferase activity
C	0000287	molecular_function	magnesium ion binding
C	0006584	biological_process	catecholamine metabolic process
C	0008171	molecular_function	O-methyltransferase activity
C	0016206	molecular_function	catechol O-methyltransferase activity
D	0000287	molecular_function	magnesium ion binding
D	0006584	biological_process	catecholamine metabolic process
D	0008171	molecular_function	O-methyltransferase activity
D	0016206	molecular_function	catechol O-methyltransferase activity
E	0000287	molecular_function	magnesium ion binding
E	0006584	biological_process	catecholamine metabolic process
E	0008171	molecular_function	O-methyltransferase activity
E	0016206	molecular_function	catechol O-methyltransferase activity
F	0000287	molecular_function	magnesium ion binding
F	0006584	biological_process	catecholamine metabolic process
F	0008171	molecular_function	O-methyltransferase activity
F	0016206	molecular_function	catechol O-methyltransferase activity
G	0000287	molecular_function	magnesium ion binding
G	0006584	biological_process	catecholamine metabolic process
G	0008171	molecular_function	O-methyltransferase activity
G	0016206	molecular_function	catechol O-methyltransferase activity
H	0000287	molecular_function	magnesium ion binding
H	0006584	biological_process	catecholamine metabolic process
H	0008171	molecular_function	O-methyltransferase activity
H	0016206	molecular_function	catechol O-methyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue 6PS A 301

Chain	Residue
A	GLY66
A	TRP143
A	ARG146
A	MET89
A	GLU90
A	ILE91
A	GLY117
A	SER119
A	GLN120
A	ASP141
A	HIS142

site_id	AC2
Number of Residues	10
Details	binding site for residue PO4 A 302

Chain	Residue
A	SER186
A	SER187
A	HOH403
A	HOH406
A	HOH435
C	SER216
D	THR4
D	LYS5
D	GLU6
D	CXS302

site_id	AC3
Number of Residues	6
Details	binding site for residue PO4 A 303

Chain	Residue
A	TYR194
A	HOH401
A	HOH404
A	HOH464
F	TYR194
F	HOH410

site_id	AC4
Number of Residues	3
Details	binding site for residue PO4 A 304

Chain	Residue
A	TRP143
A	LYS144
A	HOH434

site_id	AC5
Number of Residues	6
Details	binding site for residue K A 305

Chain	Residue
A	VAL183
A	ARG184
A	SER186
A	PHE189
A	HOH473
F	TYR197

site_id	AC6
Number of Residues	6
Details	binding site for residue K A 306

Chain	Residue
A	TYR197
F	VAL183
F	ARG184
F	SER186
F	PHE189
F	HOH496

site_id	AC7
Number of Residues	12
Details	binding site for residue 6PS B 301

Chain	Residue
B	MET40
B	GLY66
B	MET89
B	GLU90
B	ILE91
B	GLY117
B	ALA118
B	SER119
B	GLN120
B	ASP141
B	HIS142
B	TRP143

site_id	AC8
Number of Residues	10
Details	binding site for residue PO4 B 302

Chain	Residue
B	SER186
B	SER187
B	HOH404
B	HOH405
E	SER216
H	THR4
H	LYS5
H	GLU6
H	CXS302
H	HOH433

site_id	AC9
Number of Residues	4
Details	binding site for residue PO4 B 303

Chain	Residue
B	TYR194
B	HOH444
B	HOH458
G	TYR194

site_id	AD1
Number of Residues	3
Details	binding site for residue PO4 B 304

Chain	Residue
B	TRP143
B	LYS144
F	LYS129

site_id	AD2
Number of Residues	3
Details	binding site for residue PO4 B 305

Chain	Residue
B	GLY83
B	ARG85
B	LYS111

site_id	AD3
Number of Residues	6
Details	binding site for residue K B 306

Chain	Residue
B	VAL183
B	ARG184
B	SER186
B	PHE189
B	HOH511
G	TYR197

site_id	AD4
Number of Residues	6
Details	binding site for residue K B 308

Chain	Residue
B	TYR197
G	VAL183
G	ARG184
G	SER186
G	PHE189
G	HOH464

site_id	AD5
Number of Residues	9
Details	binding site for residue 6PS C 301

Chain	Residue
C	GLY66
C	MET89
C	GLU90
C	ILE91
C	GLY117
C	SER119
C	GLN120
C	HIS142
C	TRP143

site_id	AD6
Number of Residues	14
Details	binding site for residue CXS C 302

Chain	Residue
C	TYR68
C	ASN92
C	TYR200
C	MET201
C	LYS202
C	PO4305
C	HOH420
F	TYR182
F	GLY185
F	SER186
C	LYS5
C	GLU6
C	ALA39
C	MET40

site_id	AD7
Number of Residues	7
Details	binding site for residue CXS C 303

Chain	Residue
C	THR176
C	PRO177
C	ASP178
C	PHE179
C	HOH444
D	GLN120
D	ARG146

site_id	AD8
Number of Residues	9
Details	binding site for residue EDO C 304

Chain	Residue
C	ASN41
C	VAL42
C	LYS46
C	ASP141
C	ASP169
C	ASN170
C	HOH415
C	HOH446
C	HOH458

site_id	AD9
Number of Residues	10
Details	binding site for residue PO4 C 305

Chain	Residue
C	THR4
C	LYS5
C	GLU6
C	CXS302
C	HOH406
C	HOH420
C	HOH452
D	SER216
F	SER186
F	SER187

site_id	AE1
Number of Residues	7
Details	binding site for residue PO4 C 306

Chain	Residue
C	ARG184
C	PHE189
C	GLU190
C	CYS191
C	K307
C	HOH407
C	HOH481

site_id	AE2
Number of Residues	5
Details	binding site for residue K C 307

Chain	Residue
C	VAL183
C	ARG184
C	SER186
C	PHE189
C	PO4306

site_id	AE3
Number of Residues	1
Details	binding site for residue CL C 308

Chain	Residue
C	HOH486

site_id	AE4
Number of Residues	9
Details	binding site for residue 6PS D 301

Chain	Residue
D	GLY66
D	MET89
D	GLU90
D	ILE91
D	GLY117
D	SER119
D	GLN120
D	HIS142
D	TRP143

site_id	AE5
Number of Residues	9
Details	binding site for residue CXS D 302

Chain	Residue
A	PO4302
A	HOH406
D	LYS5
D	GLU6
D	ALA39
D	MET40
D	ASN92
D	MET201
D	LYS202

site_id	AE6
Number of Residues	2
Details	binding site for residue EDO D 303

Chain	Residue
D	TRP143
D	HOH408

site_id	AE7
Number of Residues	5
Details	binding site for residue EDO D 304

Chain	Residue
D	LYS46
D	ASP141
D	ASP169
D	ASN170
D	LEU198

site_id	AE8
Number of Residues	5
Details	binding site for residue PO4 D 305

Chain	Residue
D	THR176
D	PRO177
D	ASP178
D	PHE179
D	HOH427

site_id	AE9
Number of Residues	3
Details	binding site for residue K D 306

Chain	Residue
D	ARG184
D	SER186
D	PHE189

site_id	AF1
Number of Residues	9
Details	binding site for residue 6PS E 301

Chain	Residue
E	MET40
E	GLY66
E	GLU90
E	ILE91
E	GLY117
E	SER119
E	GLN120
E	HIS142
E	TRP143

site_id	AF2
Number of Residues	9
Details	binding site for residue CXS E 302

Chain	Residue
E	LYS5
E	GLU6
E	ALA39
E	MET40
E	ASN92
E	LYS202
G	TYR182
G	PO4304
G	HOH455

site_id	AF3
Number of Residues	3
Details	binding site for residue CXS E 303

Chain	Residue
A	LEU10
E	ARG184
E	HIS193

site_id	AF4
Number of Residues	1
Details	binding site for residue CL E 304

Chain	Residue
E	HIS193

site_id	AF5
Number of Residues	6
Details	binding site for residue PO4 E 306

Chain	Residue
E	GLY175
E	THR176
E	PRO177
E	ASP178
E	PHE179
E	HOH418

site_id	AF6
Number of Residues	5
Details	binding site for residue K E 307

Chain	Residue
E	VAL183
E	ARG184
E	SER186
E	PHE189
E	HOH437

site_id	AF7
Number of Residues	12
Details	binding site for residue 6PS F 301

Chain	Residue
F	GLY66
F	MET89
F	GLU90
F	ILE91
F	GLY117
F	ALA118
F	SER119
F	GLN120
F	ASP141
F	HIS142
F	TRP143
F	ARG146

site_id	AF8
Number of Residues	2
Details	binding site for residue CXS F 302

Chain	Residue
F	TRP143
F	LYS144

site_id	AF9
Number of Residues	3
Details	binding site for residue PO4 F 303

Chain	Residue
F	GLN120
F	TRP143
F	ARG146

site_id	AG1
Number of Residues	12
Details	binding site for residue 6PS G 301

Chain	Residue
G	GLY66
G	TYR68
G	MET89
G	GLU90
G	ILE91
G	ALA118
G	SER119
G	GLN120
G	HIS142
G	TRP143
G	ARG146
G	PO4302

site_id	AG2
Number of Residues	4
Details	binding site for residue PO4 G 302

Chain	Residue
G	TRP143
G	LYS144
G	ASP145
G	6PS301

site_id	AG3
Number of Residues	4
Details	binding site for residue PO4 G 303

Chain	Residue
G	PRO82
G	GLY83
G	ARG85
G	LYS111

site_id	AG4
Number of Residues	9
Details	binding site for residue PO4 G 304

Chain	Residue
E	THR4
E	LYS5
E	GLU6
E	CXS302
G	SER186
G	SER187
G	SER188
G	HOH455
H	SER216

site_id	AG5
Number of Residues	10
Details	binding site for residue 6PS H 301

Chain	Residue
H	GLY66
H	TYR68
H	MET89
H	GLU90
H	ILE91
H	GLY117
H	SER119
H	GLN120
H	HIS142
H	TRP143

site_id	AG6
Number of Residues	13
Details	binding site for residue CXS H 302

Chain	Residue
B	TYR182
B	SER186
B	PO4302
B	HOH405
H	LYS5
H	GLU6
H	ALA39
H	MET40
H	TYR68
H	ASN92
H	TYR200
H	MET201
H	LYS202

site_id	AG7
Number of Residues	1
Details	binding site for residue CL H 303

Chain	Residue
H	HOH445

site_id	AG8
Number of Residues	6
Details	binding site for residue PO4 H 304

Chain	Residue
H	THR176
H	PRO177
H	ASP178
H	PHE179
H	HOH413
H	HOH415

site_id	AG9
Number of Residues	6
Details	binding site for residue PO4 H 305

Chain	Residue
C	SER58
C	GLN81
H	LEU180
H	ALA181
H	ARG184
H	HOH408

site_id	AH1
Number of Residues	5
Details	binding site for residue K H 306

Chain	Residue
H	VAL183
H	ARG184
H	SER186
H	PHE189
H	HOH448

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12237326","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	56
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 915

Chain	Residue	Details
A	ASP141	metal ligand
A	LYS144	proton shuttle (general acid/base)
A	ASP169	metal ligand
A	ASN170	metal ligand
A	GLU199	electrostatic stabiliser

site_id	MCSA2
Number of Residues	5
Details	M-CSA 915

Chain	Residue	Details
B	ASP141	metal ligand
B	LYS144	proton shuttle (general acid/base)
B	ASP169	metal ligand
B	ASN170	metal ligand
B	GLU199	electrostatic stabiliser

site_id	MCSA3
Number of Residues	5
Details	M-CSA 915

Chain	Residue	Details
C	ASP141	metal ligand
C	LYS144	proton shuttle (general acid/base)
C	ASP169	metal ligand
C	ASN170	metal ligand
C	GLU199	electrostatic stabiliser

site_id	MCSA4
Number of Residues	5
Details	M-CSA 915

Chain	Residue	Details
D	ASP141	metal ligand
D	LYS144	proton shuttle (general acid/base)
D	ASP169	metal ligand
D	ASN170	metal ligand
D	GLU199	electrostatic stabiliser

site_id	MCSA5
Number of Residues	5
Details	M-CSA 915

Chain	Residue	Details
E	ASP141	metal ligand
E	LYS144	proton shuttle (general acid/base)
E	ASP169	metal ligand
E	ASN170	metal ligand
E	GLU199	electrostatic stabiliser

site_id	MCSA6
Number of Residues	5
Details	M-CSA 915

Chain	Residue	Details
F	ASP141	metal ligand
F	LYS144	proton shuttle (general acid/base)
F	ASP169	metal ligand
F	ASN170	metal ligand
F	GLU199	electrostatic stabiliser

site_id	MCSA7
Number of Residues	5
Details	M-CSA 915

Chain	Residue	Details
G	ASP141	metal ligand
G	LYS144	proton shuttle (general acid/base)
G	ASP169	metal ligand
G	ASN170	metal ligand
G	GLU199	electrostatic stabiliser

site_id	MCSA8
Number of Residues	5
Details	M-CSA 915

Chain	Residue	Details
H	ASP141	metal ligand
H	LYS144	proton shuttle (general acid/base)
H	ASP169	metal ligand
H	ASN170	metal ligand
H	GLU199	electrostatic stabiliser

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