Current Protein Identity:Q05488 New Search
Main Difference Dimensions in This Set
Different mutation/modification Different ligand/ion Different experimental conditions

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
1BE1 GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1998-05-19 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–137(137 aa) Fragment:B12-BINDING SUBUNIT
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6;299 K;Ionic strength (raw mmCIF value) 11mM KXH3-XPO4;Pressure ATMOSPHERIC
NMR sample composition 90% H2O,10% D2O
Resolution not provided
1FMF REFINED SOLUTION STRUCTURE OF THE (13C,15N-LABELED) B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM CLOSTRIDIUM TETANOMORPHUM Deposited 2000-08-17 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–137(137 aa)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6;299 K;Ionic strength (raw mmCIF value) 11mM KXH3-XPO4;Pressure 1
NMR sample composition 1.5mM MutS U-98% 15N,13C; 11mM phosphate buffer; | 90% H2O/10% D2O
Resolution not provided
1ID8 NMR STRUCTURE OF GLUTAMATE MUTASE (B12-BINDING SUBUNIT) COMPLEXED WITH THE VITAMIN B12 NUCLEOTIDE Deposited 2001-04-04 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–137(137 aa)
Not recorded FOP 2-HYDROXY-PROPYL-AMMONIUM × 1 DBI PHOSPHORIC ACID MONO-[5-(5,6-DIMETHYL-BENZOIMIDAZOL-1-YL)-4-HYDROXY-2-HYDROXYMETHYL-TETRAHYDRO-FURAN-3-YL] ESTER × 1 SOLUTION NMR
NMR measurement conditions pH 6;299 K;Ionic strength (raw mmCIF value) 10mM potassium phosphate;Pressure ambient
NMR sample composition 1.5mM MutS U-15N; 18.0mM B12-Nucleotide; 10mM potassium phosphate buffer; 90% H2O, 10%D2O | 90% H2O/10% D2O
Resolution not provided