› 1tv3

X-ray diffraction
2.2Å resolution

Crystal structure of the N-methyl-hydroxylamine MtmB complex

Released:
DOI: 10.2210/pdb1tv3/pdb
PDB entry 1tv3 coloured by chain, front view.
PDB entry 1tv3 coloured by chain, side view.
PDB entry 1tv3 coloured by chain, top view.
Source organism: Methanosarcina barkeri
Primary publication:
Reactivity and chemical synthesis of L-pyrrolysine- the 22(nd) genetically encoded amino acid.
Hao B, Zhao G, Kang PT, Soares JA, Ferguson TK, Gallucci J, Krzycki JA, Chan MK
Chem Biol 11 1317-24 (2004)
PMID: 15380192

Function and Biology Details

Reaction catalysed: 
Methylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + ammonia
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Monomethylamine methyltransferase MtmB1 Chain: A
Molecule details ›
Chain: A
Length: 458 amino acids
Theoretical weight: 50.18 KDa
Source organism: Methanosarcina barkeri
UniProt:
  • Canonical: O30642 (Residues: 1-458; Coverage: 100%)
Gene names: mtmB, mtmB1
Sequence domains: Monomethylamine methyltransferase MtmB
Structure domains: Monomethylamine methyltransferase MtmB

Ligands and Environments

1 bound ligand:
Ligand BG4 1 x BG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1, APS BEAMLINE 14-BM-D
Spacegroup: P6322
Unit cell:
a: 157.987Å b: 157.987Å c: 136.914Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.146 0.146 0.168

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Citations

12 review citations

Radical S-adenosylmethionine enzymes.
Broderick et al. (2014)
11 more