5LQC

Crystal Structure of COMT in complex with N-[(E)-3-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-(methylamino)purin-9-yl]oxolan-2-yl]prop-2-enyl]-5-(4-fluorophenyl)-2,3-dihydroxybenzamide

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	binding site for residue 542 A 301

Chain	Residue
A	TRP38
A	SER119
A	GLN120
A	ASP141
A	HIS142
A	TRP143
A	LYS144
A	ARG146
A	ASP169
A	ASN170
A	PRO174
A	MET40
A	LEU198
A	GLU199
A	MG302
A	HOH402
A	HOH440
A	GLY66
A	TYR68
A	GLU90
A	MET91
A	TYR95
A	GLY117
A	ALA118

---

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 302

Chain	Residue
A	ASP141
A	ASP169
A	ASN170
A	542301
A	HOH402

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:12237326

Chain	Residue	Details
A	ASP141
A	VAL42
A	SER72
A	GLU90

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019

Chain	Residue	Details
A	MET91
A	SER119
A	GLU64

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
A	LYS144
A	ASP169
A	ASN170
A	GLU199
A	GLY117

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	SER216
A	SER217
A	SER221

---

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

---