Structure of PDB 3o3n Chain C

Receptor sequence
>3o3nC (length=401) Species: 1496 (Clostridioides difficile) [Search protein sequence]
KKEARVVINDLLAEQYANAFKAKEEGRPVGWSTSVFPQELAEVFDLNVLY
PENQAAGVAAKKGSLELCEIAESKGYSIDLCAYARTNFGLLENGGCEALD
MPAPDFLLCCNNICNQVIKWYENISRELDIPLIMIDTTFNNEDEVTQSRI
DYIKAQFEEAIKQLEIISGKKFDPKKFEEVMKISAENGRLWKYSMSLPAD
SSPSPMNGFDLFTYMAVIVCARGKKETTEAFKLLIEELEDNMKTGKSSFR
GEEKYRIMMEGIPCWPYIGYKMKTLAKFGVNMTGSVYPHAWALQYEVNDL
DGMAVAYSTMFNNVNLDRMTKYRVDSLVEGKCDGAFYHMNRSCKLMSLIQ
YEMQRRAAEETGLPYAGFDGDQADPRAFTNAQFETRIQGLVEVMEERKKL
N
3D structure
PDB3o3n Structural Basis for Reductive Radical Formation and Electron Recycling in (R)-2-Hydroxyisocaproyl-CoA Dehydratase.
ChainC
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.2.1.157: (R)-2-hydroxyisocaproyl-CoA dehydratase.
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 SF4 C C84 Y86 C117 C346 C81 Y83 C114 C343
BS02 IRC C N12 E55 N56 G60 K64 Y86 I116 M218 A219 I265 Y290 W294 M313 F314 N9 E52 N53 G57 K61 Y83 I113 M215 A216 I262 Y287 W291 M310 F311
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006551 L-leucine metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3o3n, PDBe:3o3n, PDBj:3o3n
PDBsum3o3n
PubMed21366233
UniProtQ5U924|HADB_CLODI (R)-2-hydroxyisocaproyl-CoA dehydratase alpha subunit (Gene Name=hadB)

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