Current Protein Identity:Q13219
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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 |
|---|---|---|---|---|---|---|---|
| 7UFG Cryo-EM structure of PAPP-A in complex with IGFBP5 Deposited 2022-03-22 | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count |
Chain A
81–1627(1547 aa)
Chain B
81–1627(1547 aa)
|
Mutation:E483A, S1144Y Mutation:E483A, S1144Y | ZN ZINC ION × 2 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 9.2;BTP (Bis-Tris-Propane) pH 9.2
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.28 Å |
| 7Y5N Structure of 1:1 PAPP-A.ProMBP complex(half map) Deposited 2022-06-17 | Assembly 1 Other combination Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count |
Chain C
81–1627(1547 aa)
Chain D
81–1627(1547 aa)
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ZN ZINC ION × 1 CA CALCIUM ION × 7 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.45 Å |
| 7Y5Q Structure of 1:1 PAPP-A.STC2 complex(half map) Deposited 2022-06-17 | Assembly 1 Insufficient information Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count |
Chain A
81–1627(1547 aa)
Chain B
81–1627(1547 aa)
|
Not recorded | ZN ZINC ION × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.80 Å |
| 8A7D Partial dimer complex of PAPP-A and its inhibitor STC2 Deposited 2022-06-20 | Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count |
Chain C
82–1617(1536 aa)
Chain Q
82–1617(1536 aa)
|
Mutation:E563Q Mutation:E563Q | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ZN ZINC ION × 1 CA CALCIUM ION × 8 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4;Hepes buffer,
20 mM Hepes pH 7.4 100 mM NaCl, 1 mM CaCl
cryo-EM vitrification conditions
Cryogen ETHANE;4 s
|
Resolution 3.06 Å |
| 8A7E PAPP-A dimer in complex with its inhibitor STC2 Deposited 2022-06-20 | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count |
Chain C
82–1617(1536 aa)
Chain Q
82–1617(1536 aa)
|
Mutation:E563Q Mutation:E563Q | ZN ZINC ION × 2 CA CALCIUM ION × 16 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4;HEPES buffer
20 mM Hepes pH 7.5 100 mM NaCl, 1mM CaCl
cryo-EM vitrification conditions
Cryogen ETHANE;Blot time 4.5 sec
|
Resolution 5.02 Å |
| 8D8O Cryo-EM structure of substrate unbound PAPP-A Deposited 2022-06-08 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
81–1627(1547 aa)
Chain B
81–1627(1547 aa)
|
Mutation:E483A, S1144Y Mutation:E483A, S1144Y | ZN ZINC ION × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 9.2;BTP (Bis-Tris-Propane) pH 9.2
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.35 Å |
| 8HGG Structure of 2:2 PAPP-A.ProMBP complex Deposited 2022-11-14 | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count |
Chain C
1–1627(1627 aa)
Chain D
1–1627(1627 aa)
|
Not recorded | ZN ZINC ION × 2 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.64 Å |
| 8HGH Structure of 2:2 PAPP-A.STC2 complex Deposited 2022-11-14 | Assembly 1 Insufficient information Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count |
Chain A
81–1627(1547 aa)
Chain B
81–1627(1547 aa)
|
Not recorded | ZN ZINC ION × 2 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.16 Å |