PDBsum entry 4js6

Lyase

PDB id: 4js6

Contents

Protein chain

257 a.a.

Ligands

MBO

Metals

_ZN

Waters ×201

PDB id:

4js6

Name:

Lyase

Title:

Crystal structure of inhibitor-free hcaii h94d

Structure:

Carbonic anhydrase 2. Chain: a. Synonym: carbonate dehydratase ii, carbonic anhydrasE C, cac, carbonic anhydrase ii, ca-ii. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ca2. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.55Å R-factor: 0.186 R-free: 0.222

Authors:

D.P.Martin,Z.S.Hann,S.M.Cohen

Key ref:

D.P.Martin et al. (2013). Metalloprotein-inhibitor binding: human carbonic anhydrase II as a model for probing metal-ligand interactions in a metalloprotein active site. Inorg Chem, 52, 12207-12215. PubMed id: 23706138 DOI: 10.1021/ic400295f

Date:

22-Mar-13 Release date: 19-Jun-13

Protein chain

P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2 from Homo sapiens

Seq: 260 a.a.

Struc: 257 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.4.2.1.1 - carbonic anhydrase.
• Reaction: hydrogencarbonate + H⁺ = CO2 + H2O
• Cofactor: Zn(2+)

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

Added reference

DOI no: 10.1021/ic400295f

Inorg Chem 52:12207-12215 (2013)

PubMed id: 23706138

Metalloprotein-inhibitor binding: human carbonic anhydrase II as a model for probing metal-ligand interactions in a metalloprotein active site.

D.P.Martin, Z.S.Hann, S.M.Cohen.

ABSTRACT

An ever-increasing number of metalloproteins are being discovered that play essential roles in physiological processes. Inhibitors of these proteins have significant potential for the treatment of human disease, but clinical success of these compounds has been limited. Herein, zinc(II)-dependent metalloprotein inhibitors in clinical use are reviewed, and the potential for using novel metal-binding groups (MBGs) in the design of these inhibitors is discussed. By using human carbonic anhydrase II as a model system, the nuances of MBG-metal interactions in the context of a protein environment can be probed. Understanding how metal coordination influences inhibitor binding may help in the design of new therapeutics targeting metalloproteins.