5K0L

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 301

Chain	Residue
A	ASN41
A	ASP141
A	ASP169
A	ASN170
A	HOH482

---

site_id	AC2
Number of Residues	13
Details	binding site for residue 6P2 A 302

Chain	Residue
A	GLU90
A	ILE91
A	GLY117
A	ALA118
A	SER119
A	GLN120
A	HIS142
A	TRP143
A	ARG146
A	ASN41
A	GLY66
A	TYR68
A	MET89

---

site_id	AC3
Number of Residues	7
Details	binding site for residue NHE A 303

Chain	Residue
A	LYS5
A	GLU6
A	ASN92
C	TRP143
C	LYS144
C	ASP145
C	HOH420

---

site_id	AC4
Number of Residues	6
Details	binding site for residue K A 304

Chain	Residue
A	VAL183
A	ARG184
A	SER186
A	PHE189
A	HOH477
A	HOH511

---

site_id	AC5
Number of Residues	5
Details	binding site for residue MG B 301

Chain	Residue
B	ASN41
B	ASP141
B	ASN170
B	HOH428
B	HOH498

---

site_id	AC6
Number of Residues	14
Details	binding site for residue 6P2 B 302

Chain	Residue
B	MET40
B	ASN41
B	GLY66
B	TYR68
B	GLU90
B	ILE91
B	GLY117
B	ALA118
B	SER119
B	GLN120
B	HIS142
B	TRP143
B	ARG146
D	6P2302

---

site_id	AC7
Number of Residues	8
Details	binding site for residue NHE B 303

Chain	Residue
B	TRP143
B	LYS144
B	ASP145
B	HOH450
D	LYS5
D	GLU6
D	TRP38
D	ASN92

---

site_id	AC8
Number of Residues	6
Details	binding site for residue K B 304

Chain	Residue
B	VAL183
B	ARG184
B	SER186
B	PHE189
B	HOH513
B	HOH534

---

site_id	AC9
Number of Residues	6
Details	binding site for residue MG C 301

Chain	Residue
C	ASN41
C	ASP141
C	ASP169
C	ASN170
C	NHE303
C	HOH401

---

site_id	AD1
Number of Residues	11
Details	binding site for residue 6P2 C 302

Chain	Residue
C	MET40
C	ASN41
C	GLY66
C	TYR68
C	GLU90
C	ILE91
C	SER119
C	GLN120
C	HIS142
C	TRP143
C	ARG146

---

site_id	AD2
Number of Residues	9
Details	binding site for residue NHE C 303

Chain	Residue
C	TRP38
C	MET40
C	ASN41
C	ASN170
C	TYR200
C	MET201
C	MG301
C	HOH433
C	HOH542

---

site_id	AD3
Number of Residues	9
Details	binding site for residue NHE C 304

Chain	Residue
A	TRP143
A	LYS144
A	ASP145
C	LYS5
C	GLU6
C	TRP38
C	CYS95
C	HOH417
C	HOH448

---

site_id	AD4
Number of Residues	5
Details	binding site for residue K C 305

Chain	Residue
C	VAL183
C	ARG184
C	SER186
C	PHE189
C	HOH506

---

site_id	AD5
Number of Residues	7
Details	binding site for residue MG D 301

Chain	Residue
D	ASN41
D	ASP141
D	LYS144
D	ASN170
D	NHE303
D	HOH402
D	HOH434

---

site_id	AD6
Number of Residues	13
Details	binding site for residue 6P2 D 302

Chain	Residue
B	6P2302
D	ASN41
D	GLY66
D	TYR68
D	MET89
D	GLU90
D	ILE91
D	GLY117
D	SER119
D	GLN120
D	HIS142
D	TRP143
D	ARG146

---

site_id	AD7
Number of Residues	8
Details	binding site for residue NHE D 303

Chain	Residue
D	TRP38
D	ASN41
D	ASN170
D	LEU198
D	TYR200
D	MG301
D	HOH464
D	HOH494

---

site_id	AD8
Number of Residues	7
Details	binding site for residue NHE D 304

Chain	Residue
B	LYS5
B	GLU6
B	CYS95
D	TRP143
D	LYS144
D	ASP145
D	HOH418

---

site_id	AD9
Number of Residues	6
Details	binding site for residue K D 305

Chain	Residue
D	VAL183
D	ARG184
D	SER186
D	PHE189
D	HOH510
D	HOH522

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
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	12
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
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

---