PDBsum entry 2q1b

Lyase

PDB id

2q1b

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Contents

			Protein chain

					256 a.a. *

			Ligands

					BEZ


					LSA

			Metals

					_ZN ×2


					_HG

			Waters ×285

* Residue conservation analysis

PDB id:

2q1b

Links

Name:

Lyase

Title:

Carbonic anhydrase ii in complex with saccharin

Structure:

Carbonic anhydrase 2. Chain: a. Synonym: carbonic anhydrase ii, carbonate dehydratase ii, ca-ii, carbonic anhydrasE C. Ec: 4.2.1.1

Source:

Homo sapiens. Human. Organism_taxid: 9606. Other_details: from human erythrocytes

Resolution:

1.70Å

R-factor:

0.149

R-free:

0.218

Authors:

G.Klebe,A.Heine,K.Koehler

Key ref:

K.Köhler et al. (2007). Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste. Angew Chem Int Ed Engl, 46, 7697-7699. PubMed id: 17705204

Date:

24-May-07

Release date:

04-Sep-07

PROCHECK

	Headers

	References

Protein chain

P00918 (CAH2_HUMAN) - Carbonic anhydrase 2 from Homo sapiens

Seq: Struc:					260 a.a. 256 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.4.2.1.1 - carbonic anhydrase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

hydrogencarbonate + H⁺ = CO2 + H2O

hydrogencarbonate	+	H(+)	=	CO2	+	H2O

Cofactor:

Zn(2+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

	Angew Chem Int Ed Engl 46:7697-7699 (2007)
PubMed id: 17705204

Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste.
K.Köhler, A.Hillebrecht, J.Schulze Wischeler, A.Innocenti, A.Heine, C.T.Supuran, G.Klebe.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21587833

M.Akkurt, S.P.Yalçın, H.Türkmen, and O.Büyükgüngör (2010).
2-Chloro-N-(4-sulfamoylphen-yl)acetamide.

Acta Crystallogr Sect E Struct Rep Online, 66, o1596.

18167490

C.T.Supuran (2008).
Carbonic anhydrases: novel therapeutic applications for inhibitors and activators.

Nat Rev Drug Discov, 7, 168-181.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.