Current Protein Identity:P80077 New Search
Main Difference Dimensions in This Set
Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1CB7 GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM RECONSTITUTED WITH METHYL-COBALAMIN Deposited 1999-03-03 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 1–483(483 aa)
Chain D 1–483(483 aa)
Not recorded COB CO-METHYLCOBALAMIN × 2 TAR D(-)-TARTARIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.5;pH 4.5
Resolution 2.00 Å R-free 0.218
1CCW STRUCTURE OF THE COENZYME B12 DEPENDENT ENZYME GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM Deposited 1999-03-01 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 1–483(483 aa) Fragment:E chain
Chain D 1–483(483 aa) Fragment:E chain
Not recorded CNC CYANOCOBALAMIN × 2 TAR D(-)-TARTARIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 4.6;pH 4.6, VAPOR DIFFUSION, HANGING DROP
Resolution 1.60 Å R-free 0.173
1I9C GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE Deposited 2001-03-19 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 1–483(483 aa)
Chain D 1–483(483 aa)
Not recorded B12 COBALAMIN × 2 5AD 5'-DEOXYADENOSINE × 2 GLU GLUTAMIC ACID × 2 2AS (2S,3S)-3-methyl-aspartic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 4.6;293 K;PEG-4000, cadmium chloride, coenzyme B12, sodium glutamate, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.90 Å R-free 0.221
6H9E Structure of glutamate mutase reconstituted with homo-coenzyme B12 Deposited 2018-08-03 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 1–483(483 aa)
Chain D 1–483(483 aa)
Not recorded B12 COBALAMIN × 2 FWK (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-ethyl-oxolane-3,4-diol × 2 TAR D(-)-TARTARIC ACID × 2 GOL GLYCEROL × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 4.5;293 K;6% (w/v) PEG-4000, 0.1 M DL-tartrate, pH=4.5, 2 mM CdCl2
Resolution 1.82 Å R-free 0.168
6H9F Structure of glutamate mutase reconstituted with bishomo-coenzyme B12 Deposited 2018-08-03 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 1–483(483 aa)
Chain D 1–483(483 aa)
Not recorded B12 COBALAMIN × 2 8ZB (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-propyl-oxolane-3,4-diol × 2 TAR D(-)-TARTARIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 4.5;293 K;6% (w/v) PEG-4000, 0.1 M DL-tartrate, pH=4.5, 2 mM CdCl2
Resolution 2.10 Å R-free 0.203