Structure of PDB 1req Chain A

Receptor sequence

>1reqA (length=727) Species: 1752 (Propionibacterium freudenreichii subsp. shermanii)

STLPRFDSVDLGNAPVPADAARRFEELAAKAGTGEAWETAEQIPVGTLFN
EDVYKDMDWLDTYAGIPPFVHGPYATMYAFRPWTIRQYAGFSTAKESNAF
YRRNLAAGQKGLSVAFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIYDMRE
LFAGIPLDQMSVSMTMNGAVLPILALYVVTAEEQGVKPEQLAGTIQNDIL
KEFMVRNTYIYPPQPSMRIISEIFAYTSANMPKWNSISISGYHMQEAGAT
ADIEMAYTLADGVDYIRAGESVGLNVDQFAPRLSFFWGIGMNFFMEVAKL
RAARMLWAKLVHQFGPKNPKSMSLRTHSQTSGWSLTAQDVYNNVVRTCIE
AMAATQGHTQSLHTNSLDEAIALPTDFSARIARNTQLFLQQESGTTRVID
PWSGSAYVEELTWDLARKAWGHIQEVEKVGGMAKAIEKGIPKMRIEEAAA
RTQARIDSGRQPLIGVNKYRLEHEPPLDVLKVDNSTVLAEQKAKLVKLRA
ERDPEKVKAALDKITWAAGNPDDKDPDRNLLKLCIDAGRAMATVGEMSDA
LEKVFGRYTAQIRTISGVYSKEVKNTPEVEEARELVEEFEQAEGRRPRIL
LAKMGQDGHDRGQKVIATAYADLGFDVDVGPLFQTPEETARQAVEADVHV
VGVSSLAGGHLTLVPALRKELDKLGRPDILITVGGVIPEQDFDELRKDGA
VEIYTPGTVIPESAISLVKKLRASLDA

3D structure

• PDB: 1req How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution.
• Chain: A
• Resolution: 2.0 Å

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

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	B12	A	Y89 L119 A139 V206 R207 E247 G333 W334 E370 A371 A373 G609 H610 D611 R612 G613 I617 Y621 S655 L657 G685 G686 Y705 T706 T709	Y88 L118 A138 V205 R206 E246 G332 W333 E369 A370 A372 G608 H609 D610 R611 G612 I616 Y620 S654 L656 G684 G685 Y704 T705 T708
BS02	DCA	A	Y75 M78 R82 T85 R87 S114 S164 T166 T195 R283 S285 H328 Q361	Y74 M77 R81 T84 R86 S113 S163 T165 T194 R282 S284 H327 Q360

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

External links

• PDB: RCSB:1req, PDBe:1req, PDBj:1req
• PDBsum: 1req
• PubMed: 8805541
• UniProt: P11653|MUTB_PROFR Methylmalonyl-CoA mutase large subunit (Gene Name=mutB)