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2foy

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2foy, resolution 1.55Å ()
Ligands: ,
Gene: CA1 (Homo sapiens)
Activity: Carbonate dehydratase, with EC number 4.2.1.1
Related: 1hcb, 2fov, 2foq, 2fos, 2fou
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

Human Carbonic Anhydrase I complexed with a two-prong inhibitor

Publication Abstract from PubMed

The atomic-resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors are reported. Each inhibitor contains a benzenesulfonamide prong and a cupric iminodiacetate (IDA-Cu(2+)) prong separated by linkers of different lengths and compositions. The ionized NH(-) group of each benzenesulfonamide coordinates to the active site Zn(2+) ion; the IDA-Cu(2+) prong of the tightest-binding inhibitor, BR30, binds to H64 of CAII and H200 of CAI. This work provides the first evidence verifying the structural basis of nanomolar affinity measured for two-prong inhibitors targeting the carbonic anhydrases.

Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors reveal the molecular basis of high affinity., Jude KM, Banerjee AL, Haldar MK, Manokaran S, Roy B, Mallik S, Srivastava DK, Christianson DW, J Am Chem Soc. 2006 Mar 8;128(9):3011-8. PMID:16506782

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2foy is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Jude KM, Banerjee AL, Haldar MK, Manokaran S, Roy B, Mallik S, Srivastava DK, Christianson DW. Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors reveal the molecular basis of high affinity. J Am Chem Soc. 2006 Mar 8;128(9):3011-8. PMID:16506782 doi:http://dx.doi.org/10.1021/ja057257n

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