Structure of PDB 2ogy Chain B

Receptor sequence

>2ogyB (length=262) Species: 1525 (Moorella thermoacetica)

MLIIGERINGMFGDIKRAIQERDPAPVQEWARRQEEGGARALDLNVGPAV
QDKVSAMEWLVEVTQEVSNLTLCLDSTNIKAIEAGLKKCKNRAMINSTNA
EREKVEKLFPLAVEHGAALIGLTMNKTGIPKDSDTRLAFAMELVAAADEF
GLPMEDLYIDPLILPANVAQDHAPEVLKTLQQIKMLADPAPKTVLGLSAV
SQNCQNRPLINRTFLAMAMACGLDAAIADACDEALIETAATAEILLNQTV
YCDSFVKMFKTR

3D structure

• PDB: 2ogy Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases.
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Enzyme Commision number: 2.1.1.258: 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	CA	B	G222 D224	G222 D224
BS02	C2F	B	M11 F12 D75 N96 D160 G196 S198 Q202 R207	M11 F12 D75 N96 D160 G196 S198 Q202 R207	MOAD: Kd=33.2uM

Gene Ontology

Molecular Function

• GO:0005509 calcium ion binding
• GO:0005515 protein binding
• GO:0008168 methyltransferase activity
• GO:0008705 methionine synthase activity
• GO:0031419 cobalamin binding
• GO:0046872 metal ion binding
• GO:0102036 methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase activity

Biological Process

• GO:0009086 methionine biosynthetic process
• GO:0015977 carbon fixation
• GO:0032259 methylation
• GO:0042558 pteridine-containing compound metabolic process
• GO:0044237 cellular metabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:2ogy, PDBe:2ogy, PDBj:2ogy
• PDBsum: 2ogy
• PubMed: 17172470
• UniProt: Q46389|ACSE_MOOTH 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase (Gene Name=acsE)