Structure of PDB 2cl5 Chain B Binding Site BS01

Receptor Information

>2cl5 Chain B (length=214) Species: 10116 (Rattus norvegicus)

MGDTKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIM
DAVIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEMNPDYAAITQ
QMLNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPD
TLLLEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEY
MKVVDGLEKAIYQG

Ligand information

• Ligand ID: BU3
• InChI: InChI=1S/C4H10O2/c1-3(5)4(2)6/h3-6H,1-2H3/t3-,4-/m1/s1
• InChIKey: OWBTYPJTUOEWEK-QWWZWVQMSA-N
• SMILES:
  OpenEye OEToolkits 1.5.0: C[C@H]([C@@H](C)O)O
  CACTVS 3.341: C[C@@H](O)[C@@H](C)O
  ACDLabs 10.04: OC(C)C(O)C
  OpenEye OEToolkits 1.5.0: CC(C(C)O)O
  CACTVS 3.341: C[CH](O)[CH](C)O
• Formula: C4 H10 O2
• Name: (R,R)-2,3-BUTANEDIOL
• ZINC: ZINC000000901616
• PDB chain: 2cl5 Chain A Residue 1220

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2cl5 Comparative Study of Ortho- and Meta-Nitrated Inhibitors of Catechol-O-Methyltransferase: Interactions with the Active Site and Regioselectivity of O-Methylation.
• Resolution: 1.6 Å
• Binding residue (original residue number in PDB): K36 E37
• Binding residue (residue number reindexed from 1): K36 E37
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): D141 K144 D169 N170 E199
• Catalytic site (residue number reindexed from 1): D141 K144 D169 N170 E199
• Enzyme Commision number: 2.1.1.6: catechol O-methyltransferase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0008171 O-methyltransferase activity
• GO:0016206 catechol O-methyltransferase activity

Biological Process

• GO:0006584 catecholamine metabolic process

External links

• PDB: RCSB:2cl5, PDBe:2cl5, PDBj:2cl5
• PDBsum: 2cl5
• PubMed: 16618795
• UniProt: P22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)