Structure of PDB 3req Chain A Binding Site BS02

Receptor Information
>3req Chain A (length=725) Species: 1752 (Propionibacterium freudenreichii subsp. shermanii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LPRFDSVDLGNAPVPADAARRFEELAAKAGTGEAWETAEQIPVGTLFNED
VYKDMDWLDTYAGIPPFVHGPYATMYAFRPWTIRQYAGFSTAKESNAFYR
RNLAAGQKGLSVAFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIYDMRELF
AGIPLDQMSVSMTMNGAVLPILALYVVTAEEQGVKPEQLAGTIQNDILKE
FMVRNTYIYPPQPSMRIISEIFAYTSANMPKWNSISISGYHMQEAGATAD
IEMAYTLADGVDYIRAGESVGLNVDQFAPRLSFFWGIGMNFFMEVAKLRA
ARMLWAKLVHQFGPKNPKSMSLRTHSQTSGWSLTAQDVYNNVVRTCIEAM
AATQGHTQSLHTNSLDEAIALPTDFSARIARNTQLFLQQESGTTRVIDPW
SGSAYVEELTWDLARKAWGHIQEVEKVGGMAKAIEKGIPKMRIEEAAART
QARIDSGRQPLIGVNKYRLEHEPPLDVLKVDNSTVLAEQKAKLVKLRAER
DPEKVKAALDKITWAAGNPDDKDPDRNLLKLCIDAGRAMATVGEMSDALE
KVFGRYTAQIRTISGVYSKEVKNTPEVEEARELVEEFEQAEGRRPRILLA
KMGQDGHDRGQKVIATAYADLGFDVDVGPLFQTPEETARQAVEADVHVVG
VSSLAGGHLTLVPALRKELDKLGRPDILITVGGVIPEQDFDELRKDGAVE
IYTPGTVIPESAISLVKKLRASLDA
Ligand information
Ligand IDADN
InChIInChI=1S/C10H13N5O4/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(18)6(17)4(1-16)19-10/h2-4,6-7,10,16-18H,1H2,(H2,11,12,13)/t4-,6-,7-,10-/m1/s1
InChIKeyOIRDTQYFTABQOQ-KQYNXXCUSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO)[CH](O)[CH]3O
ACDLabs 10.04n2c1c(ncnc1n(c2)C3OC(C(O)C3O)CO)N
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CO)O)O)N
FormulaC10 H13 N5 O4
NameADENOSINE
ChEMBLCHEMBL477
DrugBankDB00640
ZINCZINC000002169830
PDB chain3req Chain A Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3req Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		Y89 Y243 E247 G333
Binding residue
(residue number reindexed from 1)		Y86 Y240 E244 G330
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y89 Y243 H244 K604 D608 H610
Catalytic site (residue number reindexed from 1) Y86 Y240 H241 K601 D605 H607
Enzyme Commision number 5.4.99.2: methylmalonyl-CoA mutase.
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:3req, PDBe:3req, PDBj:3req
PDBsum3req
PubMed9655823
UniProtP11653|MUTB_PROFR Methylmalonyl-CoA mutase large subunit (Gene Name=mutB)

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