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PDBe Entry: 1dgf view

HUMAN ERYTHROCYTE CATALASE
Summary
Header OXIDOREDUCTASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.5 Å, R-factor: 17.4%, Free R-factor: 19.2%, Spacegroup: P 21 21 21
Released 11/02/2000, deposition: 24/11/1999, last revision: 24/02/2009
Authors Putnam, C.D.search; Arvai, A.S.search; Bourne, Y.search; Tainer, J.A.search
Primary citation Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism.
J.MOL.BIOL.search vol:296, pag:295-309 (2000) [PubMed ID 10656833 ]search
Keywords CATALASEsearch, HEMEsearch, NADPHsearch, HYDROGEN PEROXIDEsearch, OXIDOREDUCTASEsearch
EC 1.11.1.6 ExPASy BRENDA search (A B C D)
Organism Homo sapiens(human) 9606search(A B C D)
UniProt Catalase (EC 1.11.1.6) P04040search (A B C D)
Solvent A, B, C, D
Related entries 1dgb, 1dgg, 1dgh
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D CATALASE Protein P04040 (CATA_HUMAN)search
497 100%
Heterogens
Id Name Ligands
A, C, B, D ACETATE ION ACT search
A, B, C, D PROTOPORPHYRIN IX CONTAINING FE HEM search
A, C NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE NDP search
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