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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：P17813 New Search
3PDB entries
3Biological assembly
3chain/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
5HZV Crystal structure of the zona pellucida module of human endoglin/CD105 Deposited 2016-02-03 Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 338–581（244 aa）
Mutation：;D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N,D449A, K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, D730A AND R734N ; GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；11.5% equal mixture of MPD, PEG 1000 and PEG 3350 (1:1:1), MES/imidazole mix
Resolution 2.70 Å R-free 0.272
5HZW Crystal structure of the orphan region of human endoglin/CD105 in complex with BMP9 Deposited 2016-02-03 Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 26–337（312 aa） Fragment：UNP Residues 27-393,UNP Residues 25-337,UNP Residues 27-393,UNP Residues 25-337
Mutation：;I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N ; NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.1 M AMMONIUM TARTRATE
Resolution 4.45 Å R-free 0.318
5I04 Crystal structure of the orphan region of human endoglin/CD105 Deposited 2016-02-03 Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 26–337（312 aa）
Mutation：;I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N,I57T, D137A, K138A, E227A, N228A, A270H, K274H, K294A, A367V, I372V, E414A, E417A, D418A, R422N ; NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PGE TRIETHYLENE GLYCOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；30% PEG 1000, 0.1 M TRIS-HCL
Resolution 2.42 Å R-free 0.263

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.