1q7l Summary


Zn-binding domain of the T347G mutant of human aminoacylase-I

The structure was published by Lindner, H.A., Lunin, V.V., Alary, A., Hecker, R., Cygler, M., and Menard, R., in 2003 in a paper entitled "Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.4 Å and deposited in 2003.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Aminoacylase-1.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 Aminoacylase-1 Q03154 (1-198) (ACY1_HUMAN)search Homo sapienssearch < 90% 198 96%
C Aminoacylase-1 Q03154 (1-198) (ACY1_HUMAN)search Homo sapienssearch < 90% 198 96%
B Aminoacylase-1 Q03154 (321-408) (ACY1_HUMAN)search Homo sapienssearch < 90% 88 100%
D Aminoacylase-1 Q03154 (321-408) (ACY1_HUMAN)search Homo sapienssearch < 90% 88 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q03154 (1 - 198) Aminoacylase-1 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, C Bacterial dinuclear zinc exopeptidasessearch Zn peptidasessearch Peptidase family M20/M25/M40search, Peptidase dimerisation domainsearch
B, D Bacterial dinuclear zinc exopeptidasessearch Peptidase family M20/M25/M40search

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, C (Q03154) aminoacylase activitysearch metallopeptidase activitysearch hydrolase activitysearch cellular amino acid metabolic processsearch metabolic processsearch proteolysissearch cytoplasmsearch
B, D (Q03154) hydrolase activitysearch metabolic processsearch

Chain InterPro annotation
A, C ArgE/DapE/ACY1/CPG2/YscS, conserved sitesearch Peptidase M20search N-acyl-L-amino-acid amidohydrolasesearch
B, D Peptidase M20search