Structure analysis

Crystal structure of SAM-dependent methyltransferase, possible histamine N-methyltransferase (TM1293) from Thermotoga maritima at 2.20 A resolution

X-ray diffraction
2.2Å resolution
Source organism: Thermotoga maritima MSB8
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 9507.45 Å2
Buried surface area: 140.69 Å2
Dissociation area: 70.35 Å2
Dissociation energy (ΔGdiss): 11.62 kcal/mol
Dissociation entropy (TΔSdiss): -1.11 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-194765
    Assembly 1
Confidence : 95%
No. subunits : 1
Symmetry : None
3DComplex & QSbio predictionx
No. subunits : 1
Symmetry : None
Evidence : This biological assembly agrees with the prediction of both PISA & EPPIC
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 9553.89 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-194765
    Assembly 2
Confidence : 95%
No. subunits : 1
Symmetry : None
3DComplex & QSbio predictionx
No. subunits : 1
Symmetry : None
Evidence : This biological assembly agrees with the prediction of both PISA & EPPIC

Macromolecules

Chains: A, B
Length: 219 amino acids
Theoretical weight: 25.7 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X119 (Residues: 1-207; Coverage: 100%)
Gene name: TM_1293
Pfam: Methyltransferase domain
InterPro:
CATH: Vaccinia Virus protein VP39
SCOP: UbiE/COQ5-like
PDBe-KB: UniProt Coverage View: Q9X119  
121920406080100120140160180200
 
100200
UniProt
Q9X119
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Sequence conservation

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