Structure of PDB 1req Chain C

Receptor sequence
>1reqC (length=727) Species: 1752 (Propionibacterium freudenreichii subsp. shermanii) [Search protein sequence]
STLPRFDSVDLGNAPVPADAARRFEELAAKAGTGEAWETAEQIPVGTLFN
EDVYKDMDWLDTYAGIPPFVHGPYATMYAFRPWTIRQYAGFSTAKESNAF
YRRNLAAGQKGLSVAFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIYDMRE
LFAGIPLDQMSVSMTMNGAVLPILALYVVTAEEQGVKPEQLAGTIQNDIL
KEFMVRNTYIYPPQPSMRIISEIFAYTSANMPKWNSISISGYHMQEAGAT
ADIEMAYTLADGVDYIRAGESVGLNVDQFAPRLSFFWGIGMNFFMEVAKL
RAARMLWAKLVHQFGPKNPKSMSLRTHSQTSGWSLTAQDVYNNVVRTCIE
AMAATQGHTQSLHTNSLDEAIALPTDFSARIARNTQLFLQQESGTTRVID
PWSGSAYVEELTWDLARKAWGHIQEVEKVGGMAKAIEKGIPKMRIEEAAA
RTQARIDSGRQPLIGVNKYRLEHEPPLDVLKVDNSTVLAEQKAKLVKLRA
ERDPEKVKAALDKITWAAGNPDDKDPDRNLLKLCIDAGRAMATVGEMSDA
LEKVFGRYTAQIRTISGVYSKEVKNTPEVEEARELVEEFEQAEGRRPRIL
LAKMGQDGHDRGQKVIATAYADLGFDVDVGPLFQTPEETARQAVEADVHV
VGVSSLAGGHLTLVPALRKELDKLGRPDILITVGGVIPEQDFDELRKDGA
VEIYTPGTVIPESAISLVKKLRASLDA
3D structure
PDB1req How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution.
ChainC
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y89 Y243 H244 K604 D608 H610
Catalytic site (residue number reindexed from 1) Y88 Y242 H243 K603 D607 H609
Enzyme Commision number 5.4.99.2: methylmalonyl-CoA mutase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004494 methylmalonyl-CoA mutase activity
GO:0005515 protein binding
GO:0016853 isomerase activity
GO:0016866 intramolecular transferase activity
GO:0031419 cobalamin binding
GO:0046872 metal ion binding
Biological Process
GO:0019678 propionate metabolic process, methylmalonyl pathway
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1req, PDBe:1req, PDBj:1req
PDBsum1req
PubMed8805541
UniProtP11653|MUTB_PROFR Methylmalonyl-CoA mutase large subunit (Gene Name=mutB)

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