1ogo Summary

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DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE

The structure was published by Larsson, A.M., Andersson, R., Stahlberg, J., Kenne, L., and Jones, T.A., in 2003 in a paper entitled "Dextranase from Penicillium Minioluteum. Reaction Course, Crystal Structure, and Product Complex" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.65 Å and deposited in 2003.

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

The PDB entry contains the structure of DEXTRANASE. This molecule has the UniProt identifier P48845 (DEXT_PENMI)search. The sample contained 574 residues which is 97% of the natural sequence. Out of 574 residues 572 were observed and are deposited in the PDB.

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 is most likely monomeric.

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
X DEXTRANASE P48845 (35-608) (DEXT_PENMI)search Talaromyces minioluteussearch 97% 574 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P48845 (35 - 608) DEXTRANASE Talaromyces minioluteus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
X (P48845) Dextranase, N-terminal domainsearch, Dextranase, catalytic domainsearch Dex49a from penicillium minioluteum complex, domain 1search, Single-stranded right-handed beta-helix, Pectin lyase-likesearch PF03718: Glycosyl hydrolase family 49search

Chain ID Biological process (GO) Cellular component (GO) Molecular function (GO)
X (P48845) metabolic processsearch extracellular regionsearch hydrolase activitysearch dextranase activitysearch hydrolase activity, acting on glycosyl bondssearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch

Chain InterPro annotation
X Glycoside hydrolase, family 49search Pectin lyase fold/virulence factorsearch Pectin lyase foldsearch Glycoside hydrolase, family 49, N-terminal domainsearch