Research workbench
Alpha-lytic protease complexed with C-terminal truncated pro region
Analyse Alpha-lytic protease complexed with C-terminal truncated pro region in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PRO
- Type
- protein
- Length
- 698 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-lytic protease
- UniProt
- P00778
- Ligands
- AES
- Pockets
- 7 · best druggability 0.61
Structure
x-ray diffraction · 3 distinct chains · 30% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alpha-lytic protease | protein | 198 | 7% helix, 56% strand | P00778 |
| C | Alpha-lytic protease | protein | 150 | 45% helix, 27% strand | P00778 |
| D | Alpha-lytic protease | protein | 152 | 44% helix, 27% strand | P00778 |
Ligands and binding sites
- AES · 4-(2-aminoethyl)benzenesulfonyl fluoride · ligand · 2 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 387 | 0.61 | 0.77 | 45 | empty |
| 2 | 364 | 0.59 | 0.76 | 48 | empty |
| 3 | 209 | 0.51 | 0.77 | 28 | empty |
| 4 | 211 | 0.50 | 0.76 | 28 | empty |
| 5 | 146 | 0.44 | 0.76 | 19 | AES |
Interfaces
4 interfaces between chains.
- A–C · 1359 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 1210 Ų buried · 14 hydrogen bonds · protein-protein
- C–B · 227 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 26 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 covalent (disulfide, covalent ligand).
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 P00778
- Elsewhere: RCSB PDB 3PRO · PDBe 3PRO · UniProt P00778
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