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Crystal structure of pro-S324A/D356A
Analyse Crystal structure of pro-S324A/D356A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WIV
- Type
- protein
- Length
- 1,177 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tk-subtilisin
- EC
- 3.4.21.-
- UniProt
- P58502
- Ligands
- CA
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tk-subtilisin (EC 3.4.21.-) | protein | 391 | 28% helix, 25% strand | P58502 |
| B | Tk-subtilisin (EC 3.4.21.-) | protein | 389 | 28% helix, 24% strand | P58502 |
| C | Tk-subtilisin (EC 3.4.21.-) | protein | 397 | 27% helix, 24% strand | P58502 |
Ligands and binding sites
- CA · Calcium ion · metal · 18 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1102 | 0.82 | 0.83 | 128 | empty |
| 2 | 1034 | 0.78 | 0.80 | 96 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1031 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 586 Ų buried · 2 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 P58502
- Elsewhere: RCSB PDB 3WIV · PDBe 3WIV · UniProt P58502
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