Research workbench
Crystal structure of shikimate dehydrogenase (aroe) from haemophilus influenzae
Analyse Crystal structure of shikimate dehydrogenase (aroe) from haemophilus influenzae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P77
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.95
- Source
- Haemophilus influenzae
- Molecule
- Shikimate 5-dehydrogenase
- EC
- 1.1.1.25
- UniProt
- P43876
- Ligands
- ATR
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · resolution 1.95 · 1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Shikimate 5-dehydrogenase (EC 1.1.1.25) | protein | 265 | 43% helix, 20% strand | P43876 |
Ligands and binding sites
- ATR · 2'-monophosphoadenosine-5'-diphosphate · ligand · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 389 | 0.66 | 0.79 | 39 | empty |
| 2 | 107 | 0.39 | 0.75 | 18 | empty |
| 3 | 87 | 0.35 | 0.75 | 22 | ATR |
Compared structures
- 1P77 · Crystal structure of shikimate dehydrogenase (aroe) from haemophilus influenzae · the same entry in another collection · chain A against A, TM-score 1.00
- P43876 · AlphaFold monomer V2.0 prediction for shikimate dehydrogenase (NADP(+)) (P43876) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P43876
- Elsewhere: RCSB PDB 1P77 · PDBe 1P77 · UniProt P43876
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