Structure of PDB 4req Chain A

Receptor sequence

>4reqA (length=726) Species: 1752 (Propionibacterium freudenreichii subsp. shermanii)

TLPRFDSVDLGNAPVPADAARRFEELAAKAGTGEAWETAEQIPVGTLFNE
DVYKDMDWLDTYAGIPPFVHGPYATMYAFRPWTIRQYAGFSTAKESNAFY
RRNLAAGQKGLSVAFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIYDMREL
FAGIPLDQMSVSMTMNGAVLPILALYVVTAEEQGVKPEQLAGTIQNDILK
EFMVRNTYIYPPQPSMRIISEIFAYTSANMPKWNSISISGYHMQEAGATA
DIEMAYTLADGVDYIRAGESVGLNVDQFAPRLSFFWGIGMNFFMEVAKLR
AARMLWAKLVHQFGPKNPKSMSLRTHSQTSGWSLTAQDVYNNVVRTCIEA
MAATQGHTQSLHTNSLDEAIALPTDFSARIARNTQLFLQQESGTTRVIDP
WSGSAYVEELTWDLARKAWGHIQEVEKVGGMAKAIEKGIPKMRIEEAAAR
TQARIDSGRQPLIGVNKYRLEHEPPLDVLKVDNSTVLAEQKAKLVKLRAE
RDPEKVKAALDKITWAAGNPDDKDPDRNLLKLCIDAGRAMATVGEMSDAL
EKVFGRYTAQIRTISGVYSKEVKNTPEVEEARELVEEFEQAEGRRPRILL
AKMGQDGHDRGQKVIATAYADLGFDVDVGPLFQTPEETARQAVEADVHVV
GVSSLAGGHLTLVPALRKELDKLGRPDILITVGGVIPEQDFDELRKDGAV
EIYTPGTVIPESAISLVKKLRASLDA

3D structure

• PDB: 4req Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y89 Y243 H244 K604 D608 H610
• Catalytic site (residue number reindexed from 1): Y87 Y241 H242 K602 D606 H608
• 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 H244 E247 G333 W334 E370 A371 A373 L374 G609 H610 D611 R612 G613 I617 S655 L657 G685 G686 V687 Y705 T706 T709	Y87 L117 A137 V204 R205 H242 E245 G331 W332 E368 A369 A371 L372 G607 H608 D609 R610 G611 I615 S653 L655 G683 G684 V685 Y703 T704 T707
BS02	SCA	A	Y75 M78 F81 R82 T85 R87 Y89 S164 T166 T195 Q197 R207 N236 Y243 H244 R283 S285 F287 R326 H328 Q361	Y73 M76 F79 R80 T83 R85 Y87 S162 T164 T193 Q195 R205 N234 Y241 H242 R281 S283 F285 R324 H326 Q359
BS03	MCA	A	Y75 M78 F81 R82 T85 R87 Y89 S114 S164 T166 T195 R207 N236 Y243 H244 R283 S285 F287 H328 Q330 Q361 S362	Y73 M76 F79 R80 T83 R85 Y87 S112 S162 T164 T193 R205 N234 Y241 H242 R281 S283 F285 H326 Q328 Q359 S360

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:4req, PDBe:4req, PDBj:4req
• PDBsum: 4req
• PubMed: 9655823
• UniProt: P11653|MUTB_PROFR Methylmalonyl-CoA mutase large subunit (Gene Name=mutB)