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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：P04955 New Search
3PDB entries
3Biological assembly
3chain/assembly records
Main Difference Dimensions in This Set
Different mutation/modification Different assembly state 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
1CEM ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395 Deposited 1995-12-04 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 33–395（363 aa） Fragment：CATALYTIC CORE RESIDUES 33-395
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.65 Å R-free 0.191
1IS9 Endoglucanase A from Clostridium thermocellum at atomic resolution Deposited 2001-11-26 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 33–395（363 aa） Fragment：residues 1-363
Not recorded HG MERCURY (II) ION × 6 CL CHLORIDE ION × 7 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.03 Å R-free 0.149
1KWF Atomic Resolution Structure of an Inverting Glycosidase in Complex with Substrate Deposited 2002-01-29 Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 33–395（363 aa） Fragment：catalytic core (residues 33-395)
Mutation：E95Q BGC beta-D-glucopyranose × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 0.94 Å R-free 0.113

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.