1req Summary

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METHYLMALONYL-COA MUTASE

The structure was published by Mancia, F., Keep, N.H., Nakagawa, A., et al., Bosecke, P., Diat, O., and Evans, P.R., in 1996 in a paper entitled "How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1996.

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

This PDB entry contains a complex of 2 biomacromolecules, namely METHYLMALONYL-COA MUTASE.

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 METHYLMALONYL-COA MUTASE P11653 (2-728) (MUTB_PROFR)search Propionibacterium freudenreichii subsp. shermaniisearch 100% 727 100%
C METHYLMALONYL-COA MUTASE P11653 (2-728) (MUTB_PROFR)search Propionibacterium freudenreichii subsp. shermaniisearch 100% 727 100%
B METHYLMALONYL-COA MUTASE P11652 (2-638) (MUTA_PROFR)search Propionibacterium freudenreichii subsp. shermaniisearch 100% 637 97%
D METHYLMALONYL-COA MUTASE P11652 (2-638) (MUTA_PROFR)search Propionibacterium freudenreichii subsp. shermaniisearch 100% 637 97%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P11653 (2 - 728) METHYLMALONYL-COA MUTASE Propionibacterium freudenreichii subsp. shermanii
P11652 (2 - 638) METHYLMALONYL-COA MUTASE Propionibacterium freudenreichii subsp. shermanii

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, C (P11653) Methylmalonyl-CoA mutase, N-terminal (CoA-binding) domainsearch, Cobalamin (vitamin B12)-binding domainsearch TIM Barrelsearch, Rossmann foldsearch PF01642: Methylmalonyl-CoA mutasesearch, PF02310: B12 binding domainsearch
B, D (P11652) Methylmalonyl-CoA mutase, N-terminal (CoA-binding) domainsearch, Cobalamin (vitamin B12)-binding domainsearch TIM Barrelsearch, Rossmann foldsearch PF01642: Methylmalonyl-CoA mutasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, C (P11653) protein bindingsearch cobalamin bindingsearch metal ion bindingsearch catalytic activitysearch intramolecular transferase activitysearch isomerase activitysearch methylmalonyl-CoA mutase activitysearch metabolic processsearch
B, D (P11652) cobalamin bindingsearch protein bindingsearch isomerase activitysearch metal ion bindingsearch intramolecular transferase activitysearch methylmalonyl-CoA mutase activitysearch catalytic activitysearch metabolic processsearch lactate fermentation to propionate and acetatesearch

Chain InterPro annotation
A, C Methylmalonyl-CoA mutase, alpha chain, catalyticsearch Methylmalonyl-CoA mutase, alpha/beta chain, catalyticsearch Cobalamin (vitamin B12)-binding domainsearch Methylmalonyl-CoA mutase, C-terminalsearch Cobalamin (vitamin B12)-dependent enzyme, catalytic subdomainsearch Cobalamin (vitamin B12)-dependent enzyme, catalyticsearch
B, D Methylmalonyl-CoA mutase, beta chainsearch Methylmalonyl-CoA mutase, alpha/beta chain, catalyticsearch Cobalamin (vitamin B12)-binding domainsearch Cobalamin (vitamin B12)-dependent enzyme, catalytic subdomainsearch Cobalamin (vitamin B12)-dependent enzyme, catalyticsearch Methylmalonyl-CoA mutase small subunit, N-terminalsearch