2QDY: Crystal Structure Of Fe-type Nhase From Rhodococcus Erythropolis Aj270

Citation:
Abstract
The crystal structure of Fe-type nitrile hydratase from Rhodococcus erythropolis AJ270 was determined at 1.3A resolution. The two cysteine residues (alphaCys(112) and alphaCys(114)) equatorially coordinated to the ferric ion were post-translationally modified to cysteine sulfinic acids. A glutamine residue (alphaGln(90)) in the active center gave double conformations. Based on the interactions among the enzyme, substrate and water molecules, a new mechanism of biocatalysis of nitrile hydratase was proposed, in which the water molecule activated by the glutamine residue performed as the nucleophile to attack on the nitrile which was simultaneously interacted by another water molecule coordinated to the ferric ion.
PDB ID: 2QDYDownload
MMDB ID: 64387
PDB Deposition Date: 2007/6/22
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 1.3  Å
Source Organism:
Similar Structures:
Biological Unit for 2QDY: dimeric; determined by author and by software (PISA)
Molecular Components in 2QDY
Label Count Molecule
Proteins (2 molecules)
1
Nitrile Hydratase Subunit Alpha
Molecule annotation
1
Nitrile Hydratase Subunit Beta
Molecule annotation
Chemicals (15 molecules)
1
1
2
4
3
3
4
6
5
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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