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Structure paper

TitleMolecular basis for histidine N1 position-specific methylation by CARNMT1.
Journal, issue, pagesCell Res., Vol. 28, Page 494-496, Year 2018
Publish dateSep 20, 2017 (structure data deposition date)
AuthorsCao, R. / Zhang, X. / Liu, X. / Li, Y. / Li, H.
External linksCell Res. / PubMed:29463897
MethodsX-ray diffraction
Resolution2.25 - 2.802 Å
Structure data

PDB-5yf0:
Crystal structure of CARNMT1 bound to SAM
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-5yf1:
Crystal structure of CARNMT1 bound to carnosine and SFG
Method: X-RAY DIFFRACTION / Resolution: 2.399 Å

PDB-5yf2:
Crystal structure of CARNMT1 bound to anserine and SAH
Method: X-RAY DIFFRACTION / Resolution: 2.802 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-ACT:
ACETATE ION

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SFG:
SINEFUNGIN

ChemComp-8V0:
(2~{S})-2-(3-azanylpropanoylamino)-3-(1~{H}-imidazol-4-yl)propanoic acid

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-8V3:
(2~{S})-2-(3-azanylpropanoylamino)-3-(3-methylimidazol-4-yl)propanoic acid

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / SAM / methyltransferase / complex

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