1be1 Summary



The structure was published by Tollinger, M., Konrat, R., Hilbert, B.H., Marsh, E.N., and Krautler, B., in 1998 in a paper entitled "How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum" (abstract).

The structure was determined using NMR spectroscopy and deposited in 1998.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of GLUTAMATE MUTASE. This molecule has the UniProt identifier Q05488 (GMSS_CLOTT)search. The sample contained 137 residues which is 100% of the natural sequence. Out of 137 residues 137 were observed and are deposited in the PDB.

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
A GLUTAMATE MUTASE Q05488 (1-137) (GMSS_CLOTT)search Clostridium tetanomorphumsearch 100% 137 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q05488 (1 - 137) GLUTAMATE MUTASE Clostridium tetanomorphum

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q05488) Cobalamin (vitamin B12)-binding domainsearch Rossmann foldsearch PF02310: B12 binding domainsearch

Chain ID Biological process (GO) Molecular function (GO)
A (Q05488) anaerobic glutamate catabolic processsearch glutamate catabolic process via L-citramalatesearch metal ion bindingsearch cobalamin bindingsearch intramolecular transferase activitysearch methylaspartate mutase activitysearch isomerase activitysearch

Chain InterPro annotation
A Cobalamin (vitamin B12)-binding domainsearch Methylaspartate mutase S subunitsearch