Research workbench
The structure of haemophilus influenzae IGA1 protease
Analyse The structure of haemophilus influenzae IGA1 protease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H09
- Type
- protein
- Length
- 1,925 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Immunoglobulin A1 protease
- EC
- 3.4.21.72
- UniProt
- P44969
- Ligands
- NA
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Immunoglobulin A1 protease (EC 3.4.21.72) | protein | 961 | 9% helix, 41% strand | P44969 |
| B | Immunoglobulin A1 protease (EC 3.4.21.72) | protein | 964 | 9% helix, 41% strand | P44969 |
Ligands and binding sites
- NA · Sodium ion · metal · 4 copies · chains A, B
- MLA · Malonic acid · additive · 5 copies · chains A, B
- ACT · Acetate ion · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 346 | 0.75 | 0.86 | 47 | empty |
| 2 | 363 | 0.74 | 0.86 | 46 | empty |
| 3 | 84 | 0.73 | 0.96 | 24 | ACT |
| 4 | 82 | 0.72 | 0.96 | 22 | ACT |
| 5 | 829 | 0.71 | 0.77 | 71 | empty |
Interfaces
1 interface between chains.
- A–B · 922 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3H09 · The structure of Haemophilus influenzae IgA1 protease · the same entry in another collection · chain A against A, TM-score 1.00
- P44969 · AlphaFold monomer V2.0 prediction for immunoglobulin A1 protease autotransporter (P44969) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P44969
- Elsewhere: RCSB PDB 3H09 · PDBe 3H09 · UniProt P44969
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.