Brand  (β version)

PDB ID: 1CB7

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Ligands
Code Name Style Show Link
COB Co-methylcobalamin PoSSuM
TAR D(-)-tartaric acid PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1CB7   PDBj   RCSB PDB   PDBe
Header : ISOMERASE
Title : GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM RECONSTITUTED WITH METHYL-COBALAMIN
Release Data : 2000-02-28
Compound :
mol_id molecule chains
1 PROTEIN (GLUTAMATE MUTASE) A,C
ec: 5.4.99.1
other_details: CHAINS A, C, B, D FORM HETEROTETRAMER WHICH IS THE BIOLOGICAL UNIT.
mol_id molecule chains
2 PROTEIN (GLUTAMATE MUTASE) B,D
ec: 5.4.99.1
other_details: COMPLEXED WITH CO-METHYLCOBALAMIN
Source :
mol_id organism_scientific expression_system
1 Clostridium cochlearium  (taxid:1494) Escherichia coli  (taxid:562)
atcc: DSM 1285
gene: GLMS
expression_system_strain: MC 4100, DH5 ALPHA
expression_system_plasmid: POZ3
expression_system_gene: GLMS
mol_id organism_scientific expression_system
2 Clostridium cochlearium  (taxid:1494) Escherichia coli  (taxid:562)
atcc: DSM 1285
gene: GLME
expression_system_strain: MC 4100, DH5 ALPHA
expression_system_plasmid: POZ5
expression_system_gene: GLME
Authors : Gruber, K., Reitzer, R., Kratky, C.
Keywords : GLUTAMATE MUTASE, COENZYME-B12, RADICAL REACTION, TIM-BARREL, ROSSMAN-FOLD, ISOMERASE
Exp. method : X-RAY DIFFRACTION ( 2.00 Å )
Citation :

Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights.

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

PubMed: 10467146
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

PubMed: 9757132
DOI: 10.1107/s0907444997020210

Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli.

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

PubMed: 7880251
DOI: 10.1111/j.1432-1033.1994.tb20083.x

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
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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
-