PDBsum entry 2wz0

Oxidoreductase

PDB id

2wz0

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Contents

			Protein chain

					153 a.a. *

			Ligands

					SO4 ×2


					ZZT ×2


					DMS


					DSN

			Metals

					_CU ×2


					_ZN ×3

			Waters ×307

* Residue conservation analysis

PDB id:

2wz0

Links

Name:

Oxidoreductase

Title:

L38v sod1 mutant complexed with aniline.

Structure:

Superoxide dismutase [cu-zn]. Chain: a, f. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932

Resolution:

1.72Å

R-factor:

0.198

R-free:

0.260

Authors:

S.Antonyuk,R.W.Strange,S.S.Hasnain

Key ref:

S.Antonyuk et al. (2010). Structural discovery of small molecule binding sites in Cu-Zn human superoxide dismutase familial amyotrophic lateral sclerosis mutants provides insights for lead optimization. J Med Chem, 53, 1402-1406. PubMed id: 20067275

Date:

20-Nov-09

Release date:

08-Dec-10

PROCHECK

	Headers

	References

Protein chains

P00441 (SODC_HUMAN) - Superoxide dismutase [Cu-Zn] from Homo sapiens

Seq: Struc:					154 a.a. 153 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

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



		Enzyme reactions

Enzyme class:

E.C.1.15.1.1 - superoxide dismutase.

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

Reaction:

2 superoxide + 2 H⁺ = H2O2 + O2

2 × superoxide	+	2 × H(+)	=	H2O2	+	O2

Cofactor:

Fe cation or Mn(2+) or (Zn(2+) and Cu cation)

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

Added reference

	J Med Chem 53:1402-1406 (2010)
PubMed id: 20067275

Structural discovery of small molecule binding sites in Cu-Zn human superoxide dismutase familial amyotrophic lateral sclerosis mutants provides insights for lead optimization.
S.Antonyuk, R.W.Strange, S.S.Hasnain.

ABSTRACT

Dominant inheritance of point mutations in CuZn superoxide dismutase (SOD1) is the best characterized subset of familial amyotrophic lateral sclerosis (FALS) and accounts for some 20% of the known familial cases. We report the discovery and visualization via cocrystallography of two ligand-binding pockets in human SOD1 and its pathogenic mutants that have opened up the real possibility of undertaking lead compound discovery using a fragment-based approach for therapeutic purposes for SOD1 associated motor neuron disease.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20810277

M.Chruszcz, M.Domagalski, T.Osinski, A.Wlodawer, and W.Minor (2010).
Unmet challenges of structural genomics.

Curr Opin Struct Biol, 20, 587-597.

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.