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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：P20875 New Search
3PDB entries
5Biological assembly
6chain/assembly records
Main Difference Dimensions in This Set
Different construct 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
1KJ4 SUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXES Deposited 2001-12-04 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain P 127–136（10 aa） Fragment：MATRIX-CAPSID SUBSTRATE PEPTIDE, RESIDUES 127-136
Not recorded ACT ACETATE ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Ammonium Sulphate, SODIUM PHOSPHATE, SODIUM CITRATE, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.90 Å R-free 0.248
1KJ4 SUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXES Deposited 2001-12-04 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain S 127–136（10 aa） Fragment：MATRIX-CAPSID SUBSTRATE PEPTIDE, RESIDUES 127-136
Not recorded ACT ACETATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Ammonium Sulphate, SODIUM PHOSPHATE, SODIUM CITRATE, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.90 Å R-free 0.248
1KJ4 SUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXES Deposited 2001-12-04 Assembly 3 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric（24） Consistent with protein count
Chain P 127–136（10 aa） Fragment：MATRIX-CAPSID SUBSTRATE PEPTIDE, RESIDUES 127-136
Chain S 127–136（10 aa） Fragment：MATRIX-CAPSID SUBSTRATE PEPTIDE, RESIDUES 127-136
Not recorded ACT ACETATE ION × 48 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Ammonium Sulphate, SODIUM PHOSPHATE, SODIUM CITRATE, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.90 Å R-free 0.248
1KJ7 SUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXES Deposited 2001-12-04 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain P 372–381（10 aa） Fragment：P2-NUCLEOCAPSID SUBSTRATE PEPTIDE, RESIDUES 372-381
Not recorded ACT ACETATE ION × 5 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.249
1KJF SUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXES Deposited 2001-12-04 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain P 443–452（10 aa） Fragment：p1-p6 SUBSTRATE PEPTIDE, RESIDUES 443-452
Not recorded ACT ACETATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；AMMONIUM SULPHATE, SODIUM PHOSPHATE, SODIUM CITRATE, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.251

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.