Brand  (β version)

PDB ID: 1I9C

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
2AS (2s,3s)-3-methyl-aspartic acid PoSSuM
5AD 5'-deoxyadenosine PoSSuM
B12 Cobalamin PoSSuM
GLU Glutamic acid PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 1I9C   PDBj   RCSB PDB   PDBe
Header : ISOMERASE
Title : GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE
Release Data : 2002-03-19
Compound :
mol_id molecule chains synonym
1 GLUTAMATE MUTASE A,C METHYLASPARTATE MUTASE SMALL CHAIN
ec: 5.4.99.1
mol_id molecule chains synonym
2 GLUTAMATE MUTASE B,D METHYLASPARTATE MUTASE E CHAIN
ec: 5.4.99.1
other_details: COMPLEXED WITH ADENOSYLCOBALAMAIN AND A MIXTURE OF GLUTAMATE AND 2S,3S-3-METHYLASPARTIC ACID
Source :
mol_id organism_scientific expression_system
1 Clostridium cochlearium  (taxid:1494) Escherichia coli  (taxid:562)
atcc: DSM 1285
gene: GLMS
expression_system_strain: MC4100
expression_system_plasmid: POZ3
mol_id organism_scientific expression_system
2 Clostridium cochlearium  (taxid:1494) Escherichia coli  (taxid:562)
atcc: DSM 1285
gene: GLME
expression_system_strain: DH5 ALPHA
expression_system_plasmid: POZ5
Authors : Gruber, K., Kratky, C.
Keywords : COENZYME B12, RADICAL REACTION, RIBOSE PSEUDOROTATION, TIM-BARREL, ROSSMAN-FOLD, ISOMERASE
Exp. method : X-RAY DIFFRACTION ( 1.90 Å )
Citation :

Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B(12) Dependent Enzyme Glutamate Mutase

Gruber, K.,Reitzer, R.,Kratky, C.
(2001)  Angew.Chem.Int.Ed.Engl.  40 : 3377 - 3380

PubMed: 11592143
DOI: 10.1002/1521-3773(20010917)40:18<3377::AID-ANIE3377>3.0.CO;2-8

Glutamate Mutase from Clostridum Cochlearium: The Structure of a Coenzyme B12-Dependent Enzyme Provides New Mechanistic Insights

Reitzer, R.,Gruber, K.,Jogl, G.  et al.
(1999)  Structure  7 : 891 - 902

DOI: 10.1016/S0969-2126(99)80116-6

Crystallization and Preliminary X-Ray Analysis of Recombinant Glutamate Mutase and of the Isolated Component S from Clostridium Cochlearium

Reitzer, R.,Krasser, M.,Jogl, G.  et al.
(1998)  Acta Crystallogr.,Sect.D  54 : 1039 - 1042

DOI: 10.1107/S0907444997020210

Characterization of the Coenzyme-B12-Dependent Glutamate Mutase from Clostridium Cochlearium Produced in Escherischia Coli

Zelder, O.,Beatrix, B.,Leutbecher, U.  et al.
(1994)  Eur.J.Biochem.  226 : 577 - 585

Reaction

Chain : A, C
UniProt : P80078 (GMSS_CLOCO)
Reaction: EC: Evidence:
Physiological Direction:
(2S,3S)-3-methyl-L-aspartate = L-glutamate 5.4.99.1 HAMAP-Rule:MF_00526, PubMed:7880251, PubMed:8013871
-
Chain : B, D
UniProt : P80077 (GLME_CLOCO)
Reaction: EC: Evidence:
Physiological Direction:
(2S,3S)-3-methyl-L-aspartate = L-glutamate 5.4.99.1 HAMAP-Rule:MF_01923, PubMed:1315276, PubMed:7880251
-