3M1K

Carbonic Anhydrase in complex with fragment

Summary for 3M1K

• Entry DOI: 10.2210/pdb3m1k/pdb
• Related: 2Q38 3KIG 3KNE 3M14 3M1Q 3M1W 3M2X 3M2Y 3M2Z 3MO4
• Descriptor: Carbonic anhydrase 2, ZINC ION, 1-hydroxy-2-sulfanylpyridinium, ... (5 entities in total)
• Functional Keywords: 10 stranded twisted beta-sheets, lyase, disease mutation, metal-binding
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 30357.32

Authors

Schulze Wischeler, J.,Heine, A.,Klebe, G. (deposition date: 2010-03-05, release date: 2010-11-17, Last modification date: 2024-02-28)

Primary citation

Schulze Wischeler, J.,Innocenti, A.,Vullo, D.,Agrawal, A.,Cohen, S.M.,Heine, A.,Supuran, C.T.,Klebe, G.
Bidentate Zinc chelators for alpha-carbonic anhydrases that produce a trigonal bipyramidal coordination geometry.
Chemmedchem, 5:1609-1615, 2010

PubMed Abstract: A series of new zinc binding groups (ZBGs) has been evaluated kinetically on 13 carbonic anhydrase (CA) isoforms. The fragments show affinity for all isoforms with IC(50) values in the range of 2-11 microM. The crystal structure of hCA II in complex with one such fragment reveals a bidentate binding mode with a trigonal-bipyramidal coordination geometry at the Zn(2+) center. The fragment also interacts with Thr199 and Thr200 through hydrogen bonding and participates in a water network. Further development of this ZBG should increase the binding affinity leading to a structurally distinct and promising class of CA inhibitors.

PubMed: 20629007
DOI: 10.1002/cmdc.201000200

Experimental method

X-RAY DIFFRACTION (1.35 Å)