Brand  (β version)

PDB ID: 1EQ2

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Ligands
Code Name Style Show Link
NAP Nadp nicotinamide-adenine-dinucleotide phosphate PoSSuM
ADQ Adenosine-5'-diphosphate-glucose PoSSuM
Non-standard Residues
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CSO S-hydroxycysteine
Glycosylation
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Structure summary

Code : 1EQ2   PDBj   RCSB PDB   PDBe
Header : ISOMERASE
Title : THE CRYSTAL STRUCTURE OF ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE
Release Data : 2000-11-08
Compound :
mol_id molecule chains
1 ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE A,B,C,D,E,F,G,H,I,J
ec: 5.1.3.20
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
expression_system_plasmid: PT7-5
Authors : Deacon, A.M., Ni, Y.S., Coleman Jr., W.G., Ealick, S.E.
Keywords : N-terminal domain Rossmann fold, C-terminal mixed alpha/beta domain, Short-chain dehydrogenase/reductase fold, ISOMERASE
Exp. method : X-RAY DIFFRACTION ( 2.0 Å )
Citation :

The crystal structure of ADP-L-glycero-D-mannoheptose 6-epimerase: catalysis with a twist.

Deacon, A.M.,Ni, Y.S.,Coleman Jr., W.G.  et al.
(2000)  Structure Fold.Des.  8 : 453 - 462

PubMed: 10896473
DOI: 10.1016/S0969-2126(00)00128-3

Crystallization and Preliminary X-ray Diffraction Studies of the Lipopolysaccharide Core Biosynthetic Enzyme ADP-L-glycero-D-mannoheptose 6-epimerase from Escherichia coli K-12

Ding, L.,Zhang, Y.,Deacon, A.M.  et al.
(1999)  Acta Crystallogr.,Sect.D  55 : 685 - 688

DOI: 10.1107/S0907444998014723

Reaction

Chain : A, B, C, D, E, F, G, H, I, J
UniProt : P67910 (HLDD_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D- manno-heptose 5.1.3.20 PubMed:7929099
-
Cofactor: Evidence: Note:
NAD(+) ECO:0000269 | PubMed:11313358
ECO:0000269 | PubMed:7929099
ECO:0000269 | PubMed:11313358
ECO:0000269 | PubMed:7929099
Binds 1 NADP(+) per subunit. NAD(+) can substitute for NADP(+), but enzymatic activity is reduced.