Research workbench
Active form of human pai-1
Analyse Active form of human pai-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DVM
- Type
- protein
- Length
- 1,476 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Plasminogen activator inhibitor-1
- UniProt
- P05121
- Ligands
- CL
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 29% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Plasminogen activator inhibitor-1 | protein | 375 | 29% helix, 31% strand | P05121 |
| B | Plasminogen activator inhibitor-1 | protein | 365 | 29% helix, 31% strand | P05121 |
| C | Plasminogen activator inhibitor-1 | protein | 364 | 28% helix, 31% strand | P05121 |
| D | Plasminogen activator inhibitor-1 | protein | 372 | 29% helix, 31% strand | P05121 |
Ligands and binding sites
- CL · Chloride ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.74 | 0.77 | 80 | empty |
| 2 | 759 | 0.72 | 0.78 | 73 | CL |
| 3 | 507 | 0.68 | 0.79 | 42 | empty |
| 4 | 225 | 0.60 | 0.80 | 30 | empty |
| 5 | 136 | 0.57 | 0.83 | 24 | empty |
Interfaces
4 interfaces between chains.
- C–D · 839 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 804 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 368 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 48 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P05121
- Elsewhere: RCSB PDB 1DVM · PDBe 1DVM · UniProt P05121
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