2AQM	Oxidoreductase	date	Aug 18, 2005
title	Cuzn Superoxide Dismutase From Brucella Abortus
authors	M.Didonato, C.J.Kassmann, C.K.Bruns, D.E.Cabelli, Z.Cao, L.B.Tabatabai, J.S.Kroll, E.D.Getzoff
compound		source
Molecule: Superoxide Dismutase [Cu-Zn] Chain: A Ec: 1.15.1.1 Engineered: Yes		Organism_scientific: Brucella Abortus Organism_common: Bacteria Gene: Sodc Expression_system: Escherichia Coli Expression_system_common: Bacteria
symmetry	Space Group: I 2 2 2	R_factor
crystal cell	length a length b length c angle alpha angle beta angle gamma 49.910 70.528 80.359 90.00 90.00 90.00
method	X-Ray Diffraction	resolution	1.10 Å
ligand	CU1, GOL, SO4, ZN	enzyme	Oxidoreductase E.C.1.15.1.1 BRENDA
Gene	BRUAB2 ; SODC (B. abortus)
Gene Ontology	Chain Function Process Component A superoxide dismutase activit... copper, zinc superoxide dism... copper ion binding zinc ion binding antioxidant activity oxidoreductase activity metal ion binding superoxide metabolic process... periplasmic space

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (62 Kb) [Save to disk] Biological Unit Coordinates (2aqm.pdb1.gz) 58 Kb CSU: Contacts of Structural Units for 2AQM Likely Quarternary Molecular Structure file(s) for 2AQM Structure Factors (504 Kb) Retrieve 2AQM in mmCIF format [Save to disk]

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Structure-derived information

Electron Density related parameters from EDS Electron Density Server, at Upsala Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 2AQM, from MSDmotif at EBI Fold representative 2aqm from FSSP and Dali (Families of Structurally Similar Proteins)

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [2aqm_A]

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