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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：P56734 New Search
11PDB entries
14Biological assembly
34chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
1Y52 structure of insect cell (Baculovirus) expressed AVR4 (C122S)-biotin complex Deposited 2004-12-02 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain X 25–150（126 aa）
Chain Y 25–150（126 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 BTN BIOTIN × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；2.0M ammonium sulfate,0.1M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.70 Å R-free 0.200
1Y53 Crystal structure of bacterial expressed avidin related protein 4 (AVR4) C122S Deposited 2004-12-02 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain X 25–150（126 aa）
Chain Y 25–150（126 aa）
Mutation：C122S Mutation：C122S FMT FORMIC ACID × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；2M sodium formate, 0.1M sodium acetate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.20 Å R-free 0.185
1Y55 Crystal structure of the C122S mutant of E. Coli expressed avidin related protein 4 (AVR4)-biotin complex Deposited 2004-12-02 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain X 25–150（126 aa）
Chain Y 25–150（126 aa）
Mutation：C122S Mutation：C122S BTN BIOTIN × 4 FMT FORMIC ACID × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；2M sodium formate, 0.1M sodium acetate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.00 Å R-free 0.177
2FHL avidin related protein (AVR4)-BNA complex Deposited 2005-12-26 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 25–145（121 aa）
Chain B 25–145（121 aa）
Mutation：C122S Mutation：C122S BNI 5-(2-OXO-HEXAHYDRO-THIENO[3,4-D]IMIDAZOL-6-YL)-PENTANOIC ACID (4-NITRO-PHENYL)-AMIDE × 4 FMT FORMIC ACID × 20 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；3.0M format, 0.1 M acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.05 Å R-free 0.177
2FHN Avidin related protein AVR4 (C122S, K109I mutant) in complex with BNA Deposited 2005-12-26 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain X 25–145（121 aa）
Chain Y 25–145（121 aa）
Mutation：C122S,K109I Mutation：C122S,K109I BNI 5-(2-OXO-HEXAHYDRO-THIENO[3,4-D]IMIDAZOL-6-YL)-PENTANOIC ACID (4-NITRO-PHENYL)-AMIDE × 4 FMT FORMIC ACID × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；3. M farmat, 0.1M acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.30 Å R-free 0.166
2MF6 Solution NMR structure of Chimeric Avidin, ChiAVD(I117Y), in the biotin bound form Deposited 2013-10-07 Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Chain B 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Chain C 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Chain D 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Mutation：I117Y Mutation：I117Y Mutation：I117Y Mutation：I117Y No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；333 K；Pressure 1
NMR measurement conditions pH 6.5；333 K；Pressure 1
NMR sample composition 0.7-1.2 mM [U-13C; U-15N] avidin-1, 0.7-1.2 mM d-biotin-2, 93 % H2O-3, 7 % D2O-4, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.7-1.2 mM [U-13C; U-15N] avidin-5, 0.7-1.2 mM d-biotin-6, 100 % D2O-7, 100% D2O | 100% D2O
Resolution not provided
2OF8 Crystal structure of AVR4 (D39A/C122S)-BNA complex Deposited 2007-01-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 25–150（126 aa）
Chain B 25–150（126 aa）
Mutation：D39A, C122S, D239A, C322S Mutation：D39A, C122S, D239A, C322S BNI 5-(2-OXO-HEXAHYDRO-THIENO[3,4-D]IMIDAZOL-6-YL)-PENTANOIC ACID (4-NITRO-PHENYL)-AMIDE × 4 FMT FORMIC ACID × 22 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；1.5-1.9M NaFormat, 0.1M Acetate, PH 4.2-4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.05 Å R-free 0.177
2OF9 Crystal structure of apo AVR4 (D39A/C122S) Deposited 2007-01-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 25–150（126 aa）
Chain B 25–150（126 aa）
Mutation：D39A, C122S, D239A, C322S Mutation：D39A, C122S, D239A, C322S FMT FORMIC ACID × 30 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；1.5-1.9M NaFormate, 0.1M Acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.35 Å R-free 0.192
2OFA Crystal structure of apo AVR4 (R112L,C122S) Deposited 2007-01-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 25–150（126 aa）
Chain B 25–150（126 aa）
Mutation：R112L, C122S, R312L, C322S Mutation：R112L, C122S, R312L, C322S FMT FORMIC ACID × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.4；293 K；1.5-1.9M NaFormate, 0.1M Acetate, pH 4.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.50 Å R-free 0.188
2OFB Crystal structure of AVR4 (R112L/C122S)-BNA complex Deposited 2007-01-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 25–150（126 aa）
Chain B 25–150（126 aa）
Mutation：R112L, C122S, R312L, C322S Mutation：R112L, C122S, R312L, C322S BNI 5-(2-OXO-HEXAHYDRO-THIENO[3,4-D]IMIDAZOL-6-YL)-PENTANOIC ACID (4-NITRO-PHENYL)-AMIDE × 4 FMT FORMIC ACID × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；1.5-1.9M NaFormate, 0.1M Acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.16 Å R-free 0.187
3MM0 Crystal structure of chimeric avidin Deposited 2010-04-19 Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Chain B 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Chain C 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Chain D 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Mutation：I141Y Mutation：I141Y Mutation：I141Y Mutation：I141Y No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 8.3；293 K；20% Polyethylene glycol monomethyl ether 5000, 0.1M Tris (pH 8.3), and 9mM ammonium sulfate, microbatch, temperature 293K
Resolution 2.70 Å R-free 0.309
3MM0 Crystal structure of chimeric avidin Deposited 2010-04-19 Assembly 2 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain E 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Chain F 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Chain G 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Chain H 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Mutation：I141Y Mutation：I141Y Mutation：I141Y Mutation：I141Y No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 8.3；293 K；20% Polyethylene glycol monomethyl ether 5000, 0.1M Tris (pH 8.3), and 9mM ammonium sulfate, microbatch, temperature 293K
Resolution 2.70 Å R-free 0.309
3MM0 Crystal structure of chimeric avidin Deposited 2010-04-19 Assembly 3 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain I 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Chain K 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Mutation：I141Y Mutation：I141Y No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 8.3；293 K；20% Polyethylene glycol monomethyl ether 5000, 0.1M Tris (pH 8.3), and 9mM ammonium sulfate, microbatch, temperature 293K
Resolution 2.70 Å R-free 0.309
3MM0 Crystal structure of chimeric avidin Deposited 2010-04-19 Assembly 4 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain M 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Chain N 62–82（21 aa） Fragment：P02701 Residues 25-61, 85-152 and P56734 residues 62-82
Mutation：I141Y Mutation：I141Y No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 8.3；293 K；20% Polyethylene glycol monomethyl ether 5000, 0.1M Tris (pH 8.3), and 9mM ammonium sulfate, microbatch, temperature 293K
Resolution 2.70 Å R-free 0.309

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.