3HS4

Human carbonic anhydrase II complexed with acetazolamide

Summary for 3HS4

• Entry DOI: 10.2210/pdb3hs4/pdb
• Related: 1YDA 1YDB 1YDD 1ZSB 2H4N
• Descriptor: Carbonic anhydrase 2, ZINC ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: carbonic anhydrase 2, carbonic anhydrase ii, lyase, ca ii, ca 2, acetazolamide, 5-acetamido-1, 3, 4-thiadiazole-2-sulfonamide, disease mutation, metal-binding
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 30113.30

Authors

Robbins, A.H.,Genis, C.,Domsic, J.,Sippel, K.H.,Agbandje-McKenna, M.,McKenna, R. (deposition date: 2009-06-10, release date: 2009-12-08, Last modification date: 2023-09-06)

Primary citation

Sippel, K.H.,Robbins, A.H.,Domsic, J.,Genis, C.,Agbandje-McKenna, M.,McKenna, R.
High-resolution structure of human carbonic anhydrase II complexed with acetazolamide reveals insights into inhibitor drug design.
Acta Crystallogr.,Sect.F, 65:992-995, 2009

PubMed Abstract: The crystal structure of human carbonic anhydrase II (CA II) complexed with the inhibitor acetazolamide (AZM) has been determined at 1.1 A resolution and refined to an R(cryst) of 11.2% and an R(free) of 14.7%. As observed in previous CA II-inhibitor complexes, AZM binds directly to the zinc and makes several key interactions with active-site residues. The high-resolution data also showed a glycerol molecule adjacent to the AZM in the active site and two additional AZMs that are adventitiously bound on the surface of the enzyme. The co-binding of AZM and glycerol in the active site demonstrate that given an appropriate ring orientation and substituents, an isozyme-specific CA inhibitor may be developed.

PubMed: 19851004
DOI: 10.1107/S1744309109036665

Experimental method

X-RAY DIFFRACTION (1.1 Å)