Research workbench
Ribonuclease from hericium erinaceus (RNase HE1)
Analyse Ribonuclease from hericium erinaceus (RNase HE1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GY6
- Type
- protein
- Length
- 88 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease T1
- EC
- 3.1.27.3
- UniProt
- B1Q4V2
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease T1 (EC 3.1.27.3) | protein | 88 | 14% helix, 38% strand | B1Q4V2 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 5GY6 · Ribonuclease from Hericium erinaceus (RNase He1) · 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 B1Q4V2
- Elsewhere: RCSB PDB 5GY6 · PDBe 5GY6 · UniProt B1Q4V2
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