Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
CD Cadmium ion
HCS 2-amino-4-mercapto-butyric acid
C2F 5-methyl-5,6,7,8-tetrahydrofolic acid
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1Q8J   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Cobalamin-dependent methionine synthase (1-566) from Thermotoga maritima (Cd2+, Hcy, methyltetrahydrofolate complex)
Release Data : 2004-03-23
Compound :
mol_id molecule chains
1 5-methyltetrahydrofolate S-homocysteine methyltransferase A,B
ec: 2.1.1.13
fragment: MetH_Tm (residues 1-566)
Source :
mol_id organism_scientific expression_system
1 Thermotoga maritima  (taxid:2336) Escherichia coli BL21(DE3)  (taxid:469008)
expression_system_strain: BL21-DE3
expression_system_vector_type: plasmid
expression_system_plasmid: pET29a
Authors : Evans, J.C., Huddler, D.P., Hilgers, M.T., Romanchuk, G., Matthews, R.G., Ludwig, M.L.
Keywords : homocysteine, methionine, folate, cobalamin, vitamin b12, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 1.90 Å )
Citation :

Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase.

Evans, J.C.,Huddler, D.P.,Hilgers, M.T.  et al.
(2004)  Proc.Natl.Acad.Sci.Usa  101 : 3729 - 3736

PubMed: 14752199
DOI: 10.1073/pnas.0308082100

Chain : A, B
UniProt : Q9WYA5 (Q9WYA5_THEMA)
Reaction: EC: Evidence:
Physiological Direction:
(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine 2.1.1.13 ARBA:ARBA00001700
-