Brand  (β version)

  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
MG Magnesium ion
RMN (R)-mandelic acid
SMN (S)-mandelic acid
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1MDL   PDBj   RCSB PDB   PDBe
Header : ISOMERASE
Title : MANDELATE RACEMASE MUTANT K166R CO-CRYSTALLIZED WITH (R)-MANDELATE
Release Data : 1996-10-14
Compound :
mol_id molecule chains
1 MANDELATE RACEMASE A
ec: 5.1.2.2
mutation: K166R
Source :
mol_id organism_scientific expression_system
1 Pseudomonas aeruginosa  (taxid:287) Escherichia coli  (taxid:562)
atcc: 15692
gene: MANDELATE RACEMASE
expression_system_plasmid: PKT230
expression_system_gene: MANDELATE RACEMASE
other_details: TRC PROMOTER
Authors : Clifton, J.G., Petsko, G.A.
Keywords : ISOMERASE, MANDELATE PATHWAY, MAGNESIUM
Exp. method : X-RAY DIFFRACTION ( 1.85 Å )
Citation :

Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant.

Kallarakal, A.T.,Mitra, B.,Kozarich, J.W.  et al.
(1995)  Biochemistry  34 : 2788 - 2797

PubMed: 7893690
DOI: 10.1021/bi00009a007

Mechanism of the Reaction Catalyzed by Mandelate Racemase. 2. Crystal Structure of Mandelate Racemase at 2.5-A Resolution: Identification of the Active Site and Possible Catalytic Residues

Neidhart, D.J.,Howell, P.L.,Petsko, G.A.  et al.
(1991)  Biochemistry  30 : 9264

Mandelate Racemase and Muconate Lactonizing Enzyme are Mechanistically Distinct and Structurally Homologous

Neidhart, D.J.,Kenyon, G.L.,Gerlt, J.A.  et al.
(1990)  Nature  347 : 692

Chain : A
UniProt : P11444 (MANR_PSEPU)
Reaction: EC: Evidence:
Physiological Direction:
(S)-mandelate = (R)-mandelate 5.1.2.2 PubMed:1909893, PubMed:7893689, PubMed:7893690
-