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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：P26748 New Search
6PDB entries
6Biological assembly
20chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different experimental method 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
1GP8 NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN Deposited 1999-05-11 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 264–303（40 aa） Fragment：C-TERMINAL FUNCTIONAL DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.4；293 K；Pressure 1
NMR sample composition 10% WATER/90% D2O, 99.9% D2O
Resolution not provided
2GP8 NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN Deposited 1999-05-11 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 264–303（40 aa） Fragment：C-TERMINAL FUNCTIONAL DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.4；293 K；Pressure 1
NMR sample composition 10% WATER/90% D2O, 99.9% D2O
Resolution not provided
8I1V The asymmetric unit of P22 procapsid Deposited 2023-01-13 Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric（14） Consistent with protein count
Chain H 1–303（303 aa）
Chain I 1–303（303 aa）
Chain J 1–303（303 aa）
Chain K 1–303（303 aa）
Chain L 1–303（303 aa）
Chain M 1–303（303 aa）
Chain N 1–303（303 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
9KYV The scaffold dimer of phage P22 Deposited 2024-12-09 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–303（303 aa）
Chain B 1–303（303 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.90 Å
9KYW The scaffold C-loop of phage P22 Deposited 2024-12-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 1–303（303 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.70 Å
9KYX The scaffold tetramer of phage P22 Deposited 2024-12-09 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 1–303（303 aa）
Chain B 1–303（303 aa）
Chain C 1–303（303 aa）
Chain D 1–303（303 aa）
Chain E 1–303（303 aa）
Chain F 1–303（303 aa）
Chain G 1–303（303 aa）
Chain H 1–303（303 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.90 Å

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.