› 5yf1

X-ray diffraction
2.4Å resolution

Crystal structure of CARNMT1 bound to carnosine and SFG

Released:
DOI: 10.2210/pdb5yf1/pdb
PDB entry 5yf1 coloured by chain, front view.
PDB entry 5yf1 coloured by chain, side view.
PDB entry 5yf1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis for histidine N1 position-specific methylation by CARNMT1.
Cao R, Zhang X, Liu X, Li Y, Li H
Cell Res 28 494-496 (2018)
PMID: 29463897

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + carnosine = S-adenosyl-L-homocysteine + anserine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185389 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carnosine N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 362 amino acids
Theoretical weight: 42.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8N4J0 (Residues: 53-409; Coverage: 87%)
Gene names: C9orf41, CARNMT1
Sequence domains: Carnosine N-methyltransferase

Ligands and Environments


Cofactor: Ligand SFG 2 x SFG
4 bound ligands:
Ligand 8V0 2 x 8V0
Ligand ACT 2 x ACT
Ligand EDO 3 x EDO
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P6122
Unit cell:
a: 128.125Å b: 128.125Å c: 324.643Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.168 0.201
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

METTL9 mediated N1-histidine methylation of zinc transporters is required for tumor growth.
Lv et al. (2021)
4 other articles

4 mentions without citation

Structural insights into SETD3-mediated histidine methylation on β-actin.
Guo et al. (2019)
3 more