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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：P29889 New Search
2PDB entries
4Biological assembly
8chain/assembly records
Main Difference Dimensions in This Set
Different construct 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
1MG2 MUTATION OF ALPHA PHE55 OF METHYLAMINE DEHYDROGENASE ALTERS THE REORGANIZATION ENERGY AND ELECTRONIC COUPLING FOR ITS ELECTRON TRANSFER REACTION WITH AMICYANIN Deposited 2002-08-14 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain D 631–635（5 aa）
Chain H 631–635（5 aa）
Not recorded PO4 PHOSPHATE ION × 4 CU COPPER (II) ION × 2 NA SODIUM ION × 2 HEC HEME C × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；295 K；phosphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 2.25 Å R-free 0.210
1MG2 MUTATION OF ALPHA PHE55 OF METHYLAMINE DEHYDROGENASE ALTERS THE REORGANIZATION ENERGY AND ELECTRONIC COUPLING FOR ITS ELECTRON TRANSFER REACTION WITH AMICYANIN Deposited 2002-08-14 Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain L 631–635（5 aa）
Chain P 631–635（5 aa）
Not recorded PO4 PHOSPHATE ION × 4 CU COPPER (II) ION × 2 NA SODIUM ION × 2 HEC HEME C × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；295 K；phosphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 2.25 Å R-free 0.210
1MG3 MUTATION OF ALPHA PHE55 OF METHYLAMINE DEHYDROGENASE ALTERS THE REORGANIZATION ENERGY AND ELECTRONIC COUPLING FOR ITS ELECTRON TRANSFER REACTION WITH AMICYANIN Deposited 2002-08-14 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain D 23–177（155 aa）
Chain H 23–177（155 aa）
Not recorded PO4 PHOSPHATE ION × 4 CU COPPER (II) ION × 2 NA SODIUM ION × 2 HEC HEME C × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；295 K；phosphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 2.40 Å R-free 0.246
1MG3 MUTATION OF ALPHA PHE55 OF METHYLAMINE DEHYDROGENASE ALTERS THE REORGANIZATION ENERGY AND ELECTRONIC COUPLING FOR ITS ELECTRON TRANSFER REACTION WITH AMICYANIN Deposited 2002-08-14 Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain L 23–177（155 aa）
Chain P 23–177（155 aa）
Not recorded PO4 PHOSPHATE ION × 4 CU COPPER (II) ION × 2 NA SODIUM ION × 2 HEC HEME C × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；295 K；phosphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 2.40 Å R-free 0.246

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.