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
FE9 Iron-guanylyl pyridinol cofactor
GOL Glycerol
MES 2-(N-morpholino)-ethanesulfonic acid
SO4 Sulfate ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 6GGU   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Crystal structure of native FE-hydrogenase from Methanothermobacter marburgensis
Release Data : 2019-05-22
Compound :
mol_id molecule chains synonym
1 5,10-methenyltetrahydromethanopterin hydrogenase A H(2)-dependent methylene-H(4)MPT dehydrogenase,H(2)-forming N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase,N(5),N(10)-methenyltetrahydromethanopterin hydrogenase
ec: 1.12.98.2
mutation: Wild-type
Source :
mol_id organism_scientific organism_common
1 Methanothermobacter marburgensis str. Marburg  (taxid:79929) Methanobacterium thermoautotrophicum
variant: /
cell_line: /
atcc: /
organ: /
tissue: /
Authors : Wagner, T., Huang, G., Ermler, U., Shima, S.
Keywords : [Fe]-hydrogenase, Fe-Guanylylpyridinol cofactor, H2, hydrogenase, methanogenesis, methenyl-tetrahydromethanopterin, methylene-tetrahydromethanopterin, hydrogenation, oligomerisation, protection, metalloenzyme, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 2.60 Å )
Citation :

Self-protection of the catalytic iron center of a methanogenic [Fe]-hydrogenase via a dynamic dimer-to-hexamer transformation

Wagner, T.,Huang, G.,Ermler, U.  et al.
To Be Published 

Chain : A
UniProt : P32440 (HMD_METTM)
Reaction: EC: Evidence:
Physiological Direction:
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2 = 5,10- methylenetetrahydromethanopterin + H(+) 1.12.98.2 PubMed:1521540, PubMed:1765081
right-to-left PubMed:1521540