1QWM	Oxidoreductase	date	Sep 02, 2003
title	Structure Of Helicobacter Pylori Catalase With Formic Acid Bound
authors	P.C.Loewen, X.Carpena, R.Perez-Luque, C.Rovira, R.Haas, S.Odenbreit, P.Nicholls, I.Fita
compound		source
Molecule: Kata Catalase Chain: A, B Ec: 1.11.1.6 Engineered: Yes		Organism_scientific: Helicobacter Pylori Organism_common: Bacteria Gene: Kata (Hp0875) Expression_system: Escherichia Coli Expression_system_common: Bacteria Expression_system_strain: Um255 Expression_system_vector_type: Plasmid Expression_system_plasmid: Pso100
symmetry	Space Group: P 21 21 2	R_factor	0.194
crystal cell	length a length b length c angle alpha angle beta angle gamma 64.756 154.961 96.163 90.00 90.00 90.00
method	X-Ray Diffraction	resolution	1.60 Å
ligand	AZI, FMT, HEM	enzyme	Catalase;. Equilase;. Caperase;. Optidase;. Catalase-peroxidase;. CAT. Oxidoreductase E.C.1.11.1.6 BRENDA
similarity	Belongs to the Catalase family.
catalytic activ.	2 h(2)o(2) = o(2) + 2 h(2)o.
subcellular loc.	Cytoplasm (probable).
genes	CAT (B. taurus); katE, katG (E. coli); perA (H. marismortui); katA (H. pylori); CAT (H. sapiens); katA (M. luteus); MT1959, katG (M. tuberculosis); cat-1 (N. crassa); katA (P. mirabilis); katB (P. syringae); CTA1 (S. cerevisiae)
function	Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Gene Ontology	Chain Function Process Component A, B catalase activity peroxidase activity iron ion binding oxidoreductase activity metal ion binding electron transport response to oxidative stress... hydrogen peroxide catabolic ...
disease	Acatalasemia Glycine N-Acyltransferase; Glyat
Primary reference	Structure of Helicobacter pylori catalase, with and without formic acid bound, at 1.6 A resolution., Loewen PC, Carpena X, Rovira C, Ivancich A, Perez-Luque R, Haas R, Odenbreit S, Nicholls P, Fita I, Biochemistry 2004 Mar 23;43(11):3089-103. PMID:15023060

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (208 Kb) [Save to disk] Biological Unit Coordinates (1qwm.pdb1.gz) 368 Kb CSU: Contacts of Structural Units for 1QWM Likely Quarternary Molecular Structure file(s) for 1QWM Structure Factors (970 Kb) Retrieve 1QWM in mmCIF format [Save to disk]

View 1QWM in 3D

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Visual 3D analysis of 1QWM

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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 1QWM, from MSDmotif at EBI Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1qwma_, region A [Jmol] [rasmolscript] [script source]     - Domain d1qwmb_, region B [Jmol] [rasmolscript] [script source] Fold representative 1qwm from FSSP and Dali (Families of Structurally Similar Proteins) Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH Summaries and structural analyses of PDB data files from PDBSum Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1qwm_B] [1qwm_A]

Other resources with information on 1QWM

InterPro: IPR002226 , IPR011614 MMDB (Entrez's Structure Database)

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