5K0C

Crystal Structure of COMT in complex with 2,4-dimethyl-5-[3-(2-phenylpropan-2-yl)-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

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue NHE A 301

Chain	Residue
A	TRP143
B	HOH475
A	LYS144
A	ASP145
A	HOH454
B	LYS5
B	GLU6
B	TRP38
B	ASN92
B	6OZ302

---

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 302

Chain	Residue
A	ASN92
A	HOH418
A	HOH448
B	ASN92

---

site_id	AC3
Number of Residues	4
Details	binding site for residue EDO A 303

Chain	Residue
A	ILE91
A	GLN120
A	ARG146
A	HOH423

---

site_id	AC4
Number of Residues	13
Details	binding site for residue 6OZ A 304

Chain	Residue
A	GLY66
A	MET89
A	GLU90
A	ILE91
A	GLY117
A	ALA118
A	SER119
A	GLN120
A	HIS142
A	TRP143
A	ARG146
B	NHE301
B	6OZ302

---

site_id	AC5
Number of Residues	5
Details	binding site for residue NA A 305

Chain	Residue
A	ASP141
A	ASP169
A	ASN170
A	HOH535
A	HOH539

---

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

Chain	Residue
A	VAL183
A	ARG184
A	SER186
A	PHE189
A	HOH540
A	HOH545

---

site_id	AC7
Number of Residues	10
Details	binding site for residue NHE B 301

Chain	Residue
A	LYS5
A	GLU6
A	TRP38
A	ASN92
A	6OZ304
A	HOH474
B	TRP143
B	LYS144
B	ASP145
B	HOH452

---

site_id	AC8
Number of Residues	13
Details	binding site for residue 6OZ B 302

Chain	Residue
A	NHE301
A	6OZ304
B	GLY66
B	MET89
B	GLU90
B	ILE91
B	GLY117
B	ALA118
B	SER119
B	GLN120
B	HIS142
B	TRP143
B	ARG146

---

site_id	AC9
Number of Residues	6
Details	binding site for residue NA B 303

Chain	Residue
B	VAL183
B	ARG184
B	SER186
B	PHE189
B	HOH541
B	HOH561

---

site_id	AD1
Number of Residues	4
Details	binding site for residue NA B 304

Chain	Residue
B	ASP141
B	ASP169
B	ASN170
B	HOH498

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
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	6
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	14
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
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

---