Structure of PDB 1req Chain D

Receptor sequence
>1reqD (length=622) Species: 1752 (Propionibacterium freudenreichii subsp. shermanii) [Search protein sequence]
TPTTLSLAGDFPKATEEQWEREVEKVLNRGRPPEKQLTFAECLKRLTVHT
VDGIDIVPMYRPKDAPKKLGYPGVAPFTRGTTVRNGDMDAWDVRALHEDP
DEKFTRKAILEGLERGVTSLLLRVDPDAIAPEHLDEVLSDVLLEMTKVEV
FSRYDQGAAAEALVSVYERSDKPAKDLALNLGLDPIGFAALQGTEPDLTV
LGDWVRRLAKFSPDSRAVTIDANIYHNAGAGDVAELAWALATGAEYVRAL
VEQGFTATEAFDTINFRVTATHDQFLTIARLRALREAWARIGEVFGVDED
KRGARQNAITSWRELTREDPYVNILRGSIATFSASVGGAESITTLPFTQA
LGLPEDDFPLRIARNTGIVLAEEVNIGRVNDPAGGSYYVESLTRSLADAA
WKEFQEVEKLGGMSKAVMTEHVTKVLDACNAERAKRLANRKQPITAVSEF
PMIGARSIETKPFPAAPARKGLAWHRDSEVFEQLMDRSTSVSERPKVFLA
CLGTRRDFGGREGFSSPVWHIAGIDTPQVEGGTTAEIVEAFKKSGAQVAD
LCSSAKVYAQQGLEVAKALKAAGAKALYLSGAFKEFGDDAAEAEKLIDGR
LFMGMDVVDTLSSTLDILGVAK
3D structure
PDB1req How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution.
ChainD
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) L112 N239 I240 E601 D605 A607
Catalytic site (residue number reindexed from 1) L96 N223 I224 E585 D589 A591
Enzyme Commision number 5.4.99.2: methylmalonyl-CoA mutase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 DCA D V42 R45 V26 R29
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:0019652 lactate fermentation to propionate and acetate
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
UniProtP11652|MUTA_PROFR Methylmalonyl-CoA mutase small subunit (Gene Name=mutA)

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