X-ray diffraction
1.75Å resolution

Crystal Structure of Human methyltransferase AD-003 in complex with S-adenosyl-L-homocysteine

Source organism: Homo sapiens
Entry authors: Min JR, Wu H, Zeng H, Loppnau P, Sundstrom M, Arrowsmith CH, Edwards AM, Bochkarev A, Plotnikov AN, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
(1a) S-adenosyl-L-methionine + N-terminal-(A,S)PK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-(A,S)PK-[protein]
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
N-terminal Xaa-Pro-Lys N-methyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 241 amino acids
Theoretical weight: 27.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q9BV86 (Residues: 2-223; Coverage: 100%)
Gene names: AD-003, C9orf32, METTL11A, NRMT, NRMT1, NTMT1
Sequence domains: AdoMet dependent proline di-methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

Cofactor: Ligand SAH 2 x SAH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P1
Unit cell:
a: 43.922Å b: 47.367Å c: 64.734Å
α: 105.72° β: 88.18° γ: 115.97°
R R work R free
0.197 0.194 0.258
Expression system: Escherichia coli