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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P96110 New Search
3PDB entries
3Biological assembly
18chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification 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
1B26 GLUTAMATE DEHYDROGENASE Deposited 1998-12-04 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 1–416（416 aa）
Chain B 1–416（416 aa）
Chain C 1–416（416 aa）
Chain D 1–416（416 aa）
Chain E 1–416（416 aa）
Chain F 1–416（416 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；CRYSTALLIZATION CONDITIONS: 3% POLYETHYLENE GLYCOLE, 120 MM AMMONIUM ACETATE 50 MM BIS-TRIS PROPANE PH 6.5
Resolution 3.00 Å R-free 0.295
1B3B THERMOTOGA MARITIMA GLUTAMATE DEHYDROGENASE MUTANT N97D, G376K Deposited 1998-12-07 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 2–416（415 aa）
Chain B 2–416（415 aa）
Chain C 2–416（415 aa）
Chain D 2–416（415 aa）
Chain E 2–416（415 aa）
Chain F 2–416（415 aa）
Mutation：N97D, G376K Mutation：N97D, G376K Mutation：N97D, G376K Mutation：N97D, G376K Mutation：N97D, G376K Mutation：N97D, G376K No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；6% POLYETHYLENE GLYCOLE, 120 MM AMMONIUM ACETATE, 50 MM BIS-TRIS PROPANE PH 6.5
Resolution 3.10 Å R-free 0.298
2TMG THERMOTOGA MARITIMA GLUTAMATE DEHYDROGENASE MUTANT S128R, T158E, N117R, S160E Deposited 1998-12-04 Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 2–416（415 aa）
Chain B 2–416（415 aa）
Chain C 2–416（415 aa）
Chain D 2–416（415 aa）
Chain E 2–416（415 aa）
Chain F 2–416（415 aa）
Mutation：S128R, T158E, N117R, S160E Mutation：S128R, T158E, N117R, S160E Mutation：S128R, T158E, N117R, S160E Mutation：S128R, T158E, N117R, S160E Mutation：S128R, T158E, N117R, S160E Mutation：S128R, T158E, N117R, S160E No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；6% POLYETHYLENE GLYCOLE, 120 MM AMMONIUM ACETATE, 50 MM BIS-TRIS PROPANE PH 6.5
Resolution 2.90 Å R-free 0.274

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.