Het-PDB Navi2 (PDB: 1I9C)

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Ligands
Code	Name	Link
2AS	(2s,3s)-3-methyl-aspartic acid	PoSSuM
5AD	5'-deoxyadenosine	PoSSuM
B12	Cobalamin	PoSSuM
GLU	Glutamic acid	PoSSuM

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Download interaction data: 1I9C

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

Chain :

A, C

UniProt :

P80078 (GMSS_CLOCO)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
(2S,3S)-3-methyl-L-aspartate = L-glutamate	5.4.99.1	HAMAP-Rule:MF_00526, PubMed:7880251, PubMed:8013871
(2S,3S)-3-methyl-L-aspartate = L-glutamate	-	HAMAP-Rule:MF_00526, PubMed:7880251, PubMed:8013871
Cofactor:	Evidence:	Note:
adenosylcob(III)alamin	ECO:0000255 \| HAMAP-Rule:MF_00526 ECO:0000269 \| PubMed:10467146 ECO:0000269 \| PubMed:11592143 ECO:0000269 \| PubMed:1315276 ECO:0000269 \| PubMed:7880251 ECO:0000269 \| PubMed:8013871	-

Chain :

B, D

UniProt :

P80077 (GLME_CLOCO)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
(2S,3S)-3-methyl-L-aspartate = L-glutamate	5.4.99.1	HAMAP-Rule:MF_01923, PubMed:1315276, PubMed:7880251
(2S,3S)-3-methyl-L-aspartate = L-glutamate	-	HAMAP-Rule:MF_01923, PubMed:1315276, PubMed:7880251
Cofactor:	Evidence:	Note:
adenosylcob(III)alamin	ECO:0000255 \| HAMAP-Rule:MF_01923 ECO:0000269 \| PubMed:10467146 ECO:0000269 \| PubMed:11592143 ECO:0000269 \| PubMed:1315276 ECO:0000269 \| PubMed:7880251	-

PDB ID: 1I9C

Hetero Atom Contents

Structure summary

Reaction