› 3rj7

X-ray diffraction
1.2Å resolution

Human carbonic anhydrase II complexed with its inhibitor rhenium(I)triscarbonyl-cyclopentadienyl-carboxy-4-aminomethylbenzene-sulfonamide

Released:
DOI: 10.2210/pdb3rj7/pdb
PDB entry 3rj7 coloured by chain, front view.
PDB entry 3rj7 coloured by chain, side view.
PDB entry 3rj7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
[(Cp-R)M(CO)3] (M=Re or 99mTc) Arylsulfonamide, arylsulfamide, and arylsulfamate conjugates for selective targeting of human carbonic anhydrase IX.
Can D, Spingler B, Schmutz P, Mendes F, Raposinho P, Fernandes C, Carta F, Innocenti A, Santos I, Supuran CT, Alberto R
Angew Chem Int Ed Engl 51 3354-7 (2012)
PMID: 22344779

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: 258 amino acids
Theoretical weight: 29.07 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00918 (Residues: 3-260; Coverage: 99%)
Gene name: CA2
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand MBO 1 x MBO
Ligand RCS 2 x RCS
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 42.243Å b: 41.639Å c: 72.107Å
α: 90° β: 104.55° γ: 90°
R-values:
R R work R free
0.166 0.166 0.19
Expression system: Not provided

Quick links

Citations

10 review citations

Advances in structure-based drug discovery of carbonic anhydrase inhibitors.
Supuran CT. (2017)
9 more

1 mention without citation

Trends in coordination of rhenium organometallic complexes in the Protein Data Bank.
Brink et al. (2022)