1hti

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Revision as of 10:54, 4 June 2012

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spinqualitylabelsall models PDB ID 1hti Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1hti, resolution 2.80Å ()
Ligands:
Activity:	Triose-phosphate isomerase, with EC number 5.3.1.1
Structural annotation: Resources: CATH : 1Htia00, 1Htib00 InterPro : Ipr000652, Ipr013785 Pfam : PF00121 SCOP : d1htia_, d1htib_ UniProt : P60174
Functional annotation: Biological process: glycolysis gluconeogenesis pentose-phosphate shunt fatty acid biosynthetic process lipid biosynthetic process metabolic process Molecular function: isomerase activity triose-phosphate isomerase activity catalytic activity
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

CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL ENZYME

Template:ABSTRACT PUBMED 8061610

About this Structure

1hti is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

• Mande SC, Mainfroid V, Kalk KH, Goraj K, Martial JA, Hol WG. Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme. Protein Sci. 1994 May;3(5):810-21. PMID:8061610
• Scheibel T, Bell S, Walke S. S. cerevisiae and sulfur: a unique way to deal with the environment. FASEB J. 1997 Sep;11(11):917-21. PMID:9285490