PDB Information

PDB2OGY
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourceMoorella thermoacetica
Primary Citation
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.
Doukov, T.I., Hemmi, H., Drennan, C.L., Ragsdale, S.W.
J.Biol.Chem.
HeaderTransferase
Released2007-01-09
Resolution2.300
CATH Insert Date23 Feb, 2007

PDB Images (5)

PDB Prints

PDB Chains (2)

Chain ID Date inserted into CATH CATH Status
A 23 Feb, 2007 Chopped
B 23 Feb, 2007 Chopped

CATH Domains (2)

Domain ID Date inserted into CATH Superfamily CATH Status
2ogyA00 13 Jul, 2007 3.20.20.20 Assigned
2ogyB00 14 Jul, 2007 3.20.20.20 Assigned

UniProtKB Entries (2)

Accession Gene ID Taxon Description
Q46389 ACSE_MOOTH Moorella thermoacetica 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase
Q46389 ACSE_MOOTH Moorella thermoacetica 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase
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