Research workbench
Crystal structure of the smhasa mutant H83A
Analyse Crystal structure of the smhasa mutant H83A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UYD
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemophore hasa
- UniProt
- Q54450
- Ligands
- HEM, ZN
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Hemophore hasa | protein | 174 | 24% helix, 31% strand | Q54450 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains X
- ZN · Zinc ion · metal · 8 copies · chains X
- ACT · Acetate ion · additive · 2 copies · chains X
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 | 110 | 0.52 | 0.82 | 20 | HEM |
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 Q54450
- Elsewhere: RCSB PDB 2UYD · PDBe 2UYD · UniProt Q54450
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