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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：P01023 New Search
14PDB entries
15Biological assembly
43chain/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
1AYO RECEPTOR BINDING DOMAIN OF BOVINE ALPHA-2-MACROGLOBULIN Deposited 1997-11-07 Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1338–1468（131 aa） Fragment：RECEPTOR-BINDING DOMAIN
Chain B 1338–1468（131 aa） Fragment：RECEPTOR-BINDING DOMAIN
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.9；38% PEGMMES 2000, 25 MM CACL2, 100 MM HEPES, PH 6.9
Resolution 1.90 Å R-free 0.239
1BV8 RECEPTOR DOMAIN FROM ALPHA-2-MACROGLOBULIN Deposited 1998-09-22 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1337–1474（138 aa） Fragment：RECEPTOR BINDING DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.1；298 K；Ionic strength (raw mmCIF value) 0.4；Pressure 1
Resolution not provided
2P9R Human alpha2-macroglogulin is composed of multiple domains, as predicted by homology with complement component C3 Deposited 2007-03-26 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 126–227（102 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；295 K；11% PEG 3350, 200mM di-ammonium hydrogen citrate, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.30 Å R-free 0.281
2P9R Human alpha2-macroglogulin is composed of multiple domains, as predicted by homology with complement component C3 Deposited 2007-03-26 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 126–227（102 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；295 K；11% PEG 3350, 200mM di-ammonium hydrogen citrate, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.30 Å R-free 0.281
6TAV Crystal structure of endopeptidase-induced alpha2-macroglobulin Deposited 2019-10-30 Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–1474（1474 aa）
Chain B 1–1474（1474 aa）
Chain C 1–1474（1474 aa）
Chain D 1–1474（1474 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 11 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Equivolumetric drops consisting of 0.2M tribasic ammonium citrate, pH6.4, 15% (w/v) polyethylene glycol 3350, plus 0.05M sodium fluoride as an additive, and protein solution at 4.9 absorption units at lambda=280nm yielded a single large well-shaped monocrystal after several months. This crystal could not be reproduced despite extensive trials.
Resolution 4.20 Å R-free 0.282
7O7L (h-alpha2M)4 native I Deposited 2021-04-13 Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–1474（1474 aa）
Chain B 1–1474（1474 aa）
Chain C 1–1474（1474 aa）
Chain D 1–1474（1474 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.50 Å
7O7M (h-alpha2M)4 native II Deposited 2021-04-13 Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–1474（1474 aa）
Chain B 1–1474（1474 aa）
Chain C 1–1474（1474 aa）
Chain D 1–1474（1474 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.60 Å
7O7N (h-alpha2M)4 semiactivated I state Deposited 2021-04-13 Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–1474（1474 aa）
Chain B 1–1474（1474 aa）
Chain C 1–1474（1474 aa）
Chain D 1–1474（1474 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 7.30 Å
7O7O (h-alpha2M)4 semiactivated II state Deposited 2021-04-13 Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–1474（1474 aa）
Chain B 1–1474（1474 aa）
Chain C 1–1474（1474 aa）
Chain D 1–1474（1474 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.80 Å
7O7P (h-alpha2M)4 activated state Deposited 2021-04-13 Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–1474（1474 aa）
Chain B 1–1474（1474 aa）
Chain C 1–1474（1474 aa）
Chain D 1–1474（1474 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.60 Å
7O7Q (h-alpha2M)4 trypsin-activated state Deposited 2021-04-13 Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–1474（1474 aa）
Chain B 1–1474（1474 aa）
Chain C 1–1474（1474 aa）
Chain D 1–1474（1474 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
7O7R (h-alpha2M)4 plasmin-activated I state Deposited 2021-04-13 Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–1474（1474 aa）
Chain B 1–1474（1474 aa）
Chain C 1–1474（1474 aa）
Chain D 1–1474（1474 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
7O7S (h-alpha2M)4 plasmin-activated II state Deposited 2021-04-13 Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 1–1474（1474 aa）
Chain B 1–1474（1474 aa）
Chain C 1–1474（1474 aa）
Chain D 1–1474（1474 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.30 Å
7VON Native alpha-2-macroglobulin monomer Deposited 2021-10-14 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 27–1468（1442 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 5.20 Å
7VOO Induced alpha-2-macroglobulin monomer Deposited 2021-10-14 Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 27–1335（1309 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 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.