3BWM

Crystal Structure of Human Catechol O-Methyltransferase with bound SAM and DNC

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	4
Details	BINDING SITE FOR RESIDUE MG A 300

Chain	Residue
A	ASP141
A	ASP169
A	ASN170
A	HOH411

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 303

Chain	Residue
A	ARG184
A	SER186
A	PHE189
A	HOH425
A	HOH426

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site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE SAM A 301

Chain	Residue
A	MET40
A	ASN41
A	GLY66
A	ALA67
A	TYR68
A	TYR71
A	SER72
A	GLU90
A	ILE91
A	GLY117
A	ALA118
A	SER119
A	GLN120
A	ASP141
A	HIS142
A	TRP143
A	HOH402
A	HOH441
A	HOH458

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site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE DNC A 302

Chain	Residue
A	TRP38
A	ASP141
A	HIS142
A	TRP143
A	LYS144
A	ASP169
A	ASN170
A	LEU198
A	GLU199
A	HOH411

---

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:18486144

Chain	Residue	Details
A	VAL42
A	SER72
A	GLU90
A	ASP141

---

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

Chain	Residue	Details
A	GLU64
A	ILE91
A	SER119

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	GLY117
A	LYS144
A	ASN170
A	GLU199

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:18486144

Chain	Residue	Details
A	ASP169

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1vid

Chain	Residue	Details
A	GLU199
A	LYS144

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