MolNFT v1 · #13208 · protein
Crystal structure of microplasminogen-streptokinase alpha domain complex
1L4D: “Crystal structure of microplasminogen-streptokinase alpha domain complex”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.42). MolNFT v1 #13208 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1L4D
- Type
- protein
- Length
- 361 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Plasminogen; Streptokinase
- EC
- 3.4.21.7
- UniProt
- P00747, P00779
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Plasminogen (EC 3.4.21.7) | protein | 249 | 10% helix, 35% strand | P00747 |
| B | Streptokinase | protein | 112 | 13% helix, 45% strand | P00779 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.42 | 0.77 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 726 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1L4D · Crystal structure of microplasminogen-streptokinase alpha domain complex · the same entry in another collection · chain A against A, TM-score 1.00
- P00747 · AlphaFold monomer V2.0 prediction for plasminogen (P00747) · a predicted model of the same protein · chain A against A, TM-score 0.95
- P00779 · AlphaFold monomer V2.0 prediction for streptokinase C (P00779) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 P00747
- Every structure of UniProt P00779
- Elsewhere: RCSB PDB 1L4D · PDBe 1L4D · UniProt P00747 · UniProt P00779
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