1qh5 Summary

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HUMAN GLYOXALASE II WITH S-(N-HYDROXY-N-BROMOPHENYLCARBAMOYL)GLUTATHIONE

The structure was published by Cameron, A.D., Ridderstrom, M., Olin, B., and Mannervik, B., in 1999 in a paper entitled "Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.45 Å and deposited in 1999.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of PROTEIN (HYDROXYACYLGLUTATHIONE HYDROLASE).

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PROTEIN (HYDROXYACYLGLUTATHIONE HYDROLASE) Q16775 (49-308) (GLO2_HUMAN)search Homo sapienssearch < 90% 260 100%
B PROTEIN (HYDROXYACYLGLUTATHIONE HYDROLASE) Q16775 (49-308) (GLO2_HUMAN)search Homo sapienssearch < 90% 260 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q16775 (49 - 308) PROTEIN (HYDROXYACYLGLUTATHIONE HYDROLASE) Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Glyoxalase II (hydroxyacylglutathione hydrolase)search Metallo-beta-lactamase, chain Asearch Metallo-beta-lactamase superfamilysearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (Q16775) glutathione biosynthetic processsearch hydroxyacylglutathione hydrolase activitysearch zinc ion bindingsearch

Chain InterPro annotation
A, B Beta-lactamase-likesearch Hydroxyacylglutathione hydrolasesearch