Brand  (β version)

PDB ID: 5CJT

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
5AD 5'-deoxyadenosine PoSSuM
B12 Cobalamin PoSSuM
CO6 Isobutyryl-coenzyme a PoSSuM
GDP Guanosine-5'-diphosphate PoSSuM
MG Magnesium ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 5CJT   PDBj   RCSB PDB   PDBe
Header : ISOMERASE
Title : Isobutyryl-CoA mutase fused with bound adenosylcobalamin, GDP, Mg (holo-IcmF/GDP), and substrate isobutyryl-coenzyme A
Release Data : 2015-09-09
Compound :
mol_id molecule chains
1 Isobutyryl-CoA mutase fused A,B
ec: 5.4.99.2
other_details: IcmF is misannoated as sbm in the C. metallidurans genome
Source :
mol_id organism_scientific expression_system
1 Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)  (taxid:266264) Escherichia coli BL21(DE3)  (taxid:469008)
strain: CH34 / ATCC 43123 / DSM 2839
gene: sbm, Rmet_0210
expression_system_vector_type: plasmid
expression_system_plasmid: pET28a
Authors : Jost, M., Drennan, C.L.
Keywords : Radical enzyme, complex, isomerase, G-protein chaperone
Exp. method : X-RAY DIFFRACTION ( 3.400 Å )
Citation :

Structural Basis for Substrate Specificity in Adenosylcobalamin-dependent Isobutyryl-CoA Mutase and Related Acyl-CoA Mutases.

Jost, M.,Born, D.A.,Cracan, V.  et al.
(2015)  J.Biol.Chem.  290 : 26882 - 26898

PubMed: 26318610
DOI: 10.1074/jbc.M115.676890

Reaction

Chain : A, B
UniProt : Q1LRY0 (ICMF_CUPMC)
Reaction: EC: Evidence:
Physiological Direction:
2-methylpropanoyl-CoA = butanoyl-CoA 5.4.99.13 HAMAP-Rule:MF_02050, PubMed:22167181
-
3-methylbutanoyl-CoA = 2,2-dimethylpropanoyl-CoA - PubMed:22167181
-
GTP + H2O = GDP + H(+) + phosphate - HAMAP- Rule:MF_02050, PubMed:22167181
-