› 3m1j

X-ray diffraction
1.8Å resolution

The crystal structure of a NAMI A-Carbonic Anhydrase II adduct discloses the mode of action of this novel anticancer metallodrug

Released:
DOI: 10.2210/pdb3m1j/pdb
PDB entry 3m1j coloured by chain, front view.
PDB entry 3m1j coloured by chain, side view.
PDB entry 3m1j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The x-ray structure of the adduct between NAMI-A and carbonic anhydrase provides insights into the reactivity of this metallodrug with proteins.
Casini A, Temperini C, Gabbiani C, Supuran CT, Messori L
ChemMedChem 5 1989-94 (2010)
PMID: 20931644

Function and Biology Details

Reactions catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Urea = cyanamide + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 2 Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 29.29 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00918 (Residues: 1-260; Coverage: 100%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

5 bound ligands:
Ligand ZN 1 x ZN
Ligand RU 1 x RU
Ligand MBO 1 x MBO
Ligand DMS 1 x DMS
Ligand IMD 1 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: P21
Unit cell:
a: 42.1Å b: 41.55Å c: 72.29Å
α: 90° β: 104.51° γ: 90°
R-values:
R R work R free
0.195 0.193 0.235
Expression system: Not provided

Quick links

Citations

5 review citations

Structure-activity relationships for ruthenium and osmium anticancer agents - towards clinical development.
Meier-Menches et al. (2018)
4 more