Research workbench
Structure of a cysteine hydrolase with a positive substrate
Analyse Structure of a cysteine hydrolase with a positive substrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HWH
- Type
- protein
- Length
- 175 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isochorismatase
- UniProt
- A0A0K0XHU0
- Ligands
- 66Z
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isochorismatase | protein | 175 | 33% helix, 26% strand | A0A0K0XHU0 |
Ligands and binding sites
- 66Z · (1~{S},4~{R})-3-azabicyclo[2.2.1]hept-5-en-2-one · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5HWH · Structure of a cysteine hydrolase with a positive substrate · 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 A0A0K0XHU0
- Elsewhere: RCSB PDB 5HWH · PDBe 5HWH · UniProt A0A0K0XHU0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.