6I3C

Crystal structure of Human soluble catechol O-methyltransferase in complex with 3,5-dinitrocatechol and S-adensoyl-L-methionine

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	5
Details	binding site for residue MG A 301

Chain	Residue
A	ASP141
A	ASP169
A	ASN170
A	DNC303
A	HOH423

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site_id	AC2
Number of Residues	17
Details	binding site for residue SAM A 302

Chain	Residue
A	TYR68
A	TYR71
A	SER72
A	GLU90
A	ILE91
A	SER119
A	GLN120
A	ASP141
A	HIS142
A	TRP143
A	DNC303
A	HOH436
A	HOH510
A	MET40
A	VAL42
A	GLY66
A	ALA67

---

site_id	AC3
Number of Residues	14
Details	binding site for residue DNC A 303

Chain	Residue
A	TRP38
A	ASP141
A	HIS142
A	TRP143
A	LYS144
A	ASP169
A	ASN170
A	PRO174
A	LEU198
A	GLU199
A	MG301
A	SAM302
A	HOH423
A	HOH550

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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

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P22734

Chain	Residue	Details
A	SER217

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