1cza

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spinqualitylabelsall models PDB ID 1cza Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1cza, resolution 1.90Å ()
Ligands:	, ,
Activity:	Hexokinase, with EC number 2.7.1.1
Related:	1hkb, 1hkc
Structural annotation: Resources: CATH : 1Czan02, 1Czan01, 1Czan04, 1Czan03 InterPro : Ipr001312 Pfam : PF00349, PF03727 SCOP : d1czan1, d1czan3, d1czan4, d1czan2 UniProt : P19367
Functional annotation: Cellular component: membrane mitochondrion Biological process: glycolysis Molecular function: nucleotide binding kinase activity catalytic activity transferase activity hexokinase activity ATP binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Contents 1 MUTANT MONOMER OF RECOMBINANT HUMAN HEXOKINASE TYPE I COMPLEXED WITH GLUCOSE, GLUCOSE-6-PHOSPHATE, AND ADP 2 Disease 3 About this Structure 4 See Also 5 Reference

MUTANT MONOMER OF RECOMBINANT HUMAN HEXOKINASE TYPE I COMPLEXED WITH GLUCOSE, GLUCOSE-6-PHOSPHATE, AND ADP

Template:ABSTRACT PUBMED 10686099

Disease

[HXK1_HUMAN] Defects in HK1 are the cause of hexokinase deficiency (HK deficiency) [MIM:235700]. HK deficiency is a rare autosomal recessive disease with nonspherocytic hemolytic anemia as the predominant clinical feature.

About this Structure

1cza is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

• Hexokinase

Reference

• Aleshin AE, Kirby C, Liu X, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB. Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation. J Mol Biol. 2000 Mar 3;296(4):1001-15. PMID:10686099 doi:10.1006/jmbi.1999.3494