Research workbench
Crystal structure of striga hermonthica HTL4 (SHHTL4)
Analyse Crystal structure of striga hermonthica HTL4 (SHHTL4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Z7X
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hyposensitive to light 4
- UniProt
- A0A0M4AMQ0
- Ligands
- MG
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hyposensitive to light 4 | protein | 270 | 47% helix, 17% strand | A0A0M4AMQ0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 264 | 0.76 | 0.88 | 34 | EDO, MG |
Compared structures
- 5Z7X · Crystal structure of Striga hermonthica HTL4 (ShHTL4) · the same entry in another collection · 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 A0A0M4AMQ0
- Elsewhere: RCSB PDB 5Z7X · PDBe 5Z7X · UniProt A0A0M4AMQ0
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