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PDBsum entry 3m1v
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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
3m1v

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
548 a.a. *
442 a.a. *
246 a.a. *
Ligands
F43 ×2
TP7 ×2
COM ×2
ACT ×4
PEG ×2
EDO ×3
Metals
_ZN
_MG ×9
Waters ×2516
* Residue conservation analysis
PDB id:
3m1v
Name: Transferase
Title: Structural insight into methyl-coenzyme m reductase chemistry using coenzyme b analogues
Structure: Methyl-coenzyme m reductase i subunit alpha. Chain: a, d. Synonym: mcr i alpha, coenzyme-b sulfoethylthiotransferase alpha. Methyl-coenzyme m reductase i subunit beta. Chain: b, e. Synonym: mcr i beta, coenzyme-b sulfoethylthiotransferase beta. Methyl-coenzyme m reductase i subunit gamma. Chain: c, f. Synonym: mcr i gamma, coenzyme-b sulfoethylthiotransferase gamma.
Source: Methanothermobacter marburgensis. Organism_taxid: 79929. Strain: marburg / dsm 2133. Strain: marburg / dsm 2133
Resolution:
1.45Å     R-factor:   0.136     R-free:   0.162
Authors: P.E.Cedervall,M.Dey,S.W.Ragsdale,C.M.Wilmot
Key ref: P.E.Cedervall et al. (2010). Structural insight into methyl-coenzyme M reductase chemistry using coenzyme B analogues . Biochemistry, 49, 7683-7693. PubMed id: 20707311
Date:
05-Mar-10     Release date:   15-Sep-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P11558  (MCRA_METTM) -  Methyl-coenzyme M reductase I subunit alpha from Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
Seq:
Struc: 		 
Seq:
Struc: 		550 a.a.
548 a.a.*
Protein chains
Pfam   ArchSchema ?
P11560  (MCRB_METTM) -  Methyl-coenzyme M reductase I subunit beta from Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
Seq:
Struc: 		443 a.a.
442 a.a.
Protein chains
Pfam   ArchSchema ?
P11562  (MCRG_METTM) -  Methyl-coenzyme M reductase I subunit gamma from Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
Seq:
Struc: 		249 a.a.
246 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F: E.C.2.8.4.1  - coenzyme-B sulfoethylthiotransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		Methane Biosynthesis
      Reaction: coenzyme B + methyl-coenzyme M = methane + coenzyme M-coenzyme B heterodisulfide
coenzyme B
Bound ligand (Het Group name = TP7)
corresponds exactly 		+
methyl-coenzyme M
Bound ligand (Het Group name = COM)
matches with 87.50% similarity 		= methane
 + coenzyme M-coenzyme B heterodisulfide
      Cofactor: Coenzyme F430
Coenzyme F430
Bound ligand (Het Group name = F43) matches with 96.83% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Biochemistry 49:7683-7693 (2010)
PubMed id: 20707311  
 
 
Structural insight into methyl-coenzyme M reductase chemistry using coenzyme B analogues .
P.E.Cedervall, M.Dey, A.R.Pearson, S.W.Ragsdale, C.M.Wilmot.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21525643 A.M.Orville, R.Buono, M.Cowan, A.Héroux, G.Shea-McCarthy, D.K.Schneider, J.M.Skinner, M.J.Skinner, D.Stoner-Ma, and R.M.Sweet (2011).
Correlated single-crystal electronic absorption spectroscopy and X-ray crystallography at NSLS beamline X26-C.
  J Synchrotron Radiat, 18, 358-366.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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