Research workbench
Structural changes that accompany the reduced catalytic efficiency of two semisynthetic ribonuclease analogs
Analyse Structural changes that accompany the reduced catalytic efficiency of two… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SRN
- Type
- protein
- Length
- 124 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease a
- EC
- 3.1.27.5
- UniProt
- P61823
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease a (EC 3.1.27.5) | protein | 113 | 23% helix, 33% strand | P61823 |
| B | Ribonuclease a | protein | 11 | 0% helix, 82% strand | P61823 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 910 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3SRN · Structural changes that accompany the reduced catalytic efficiency of two semisynthetic… · 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 P61823
- Elsewhere: RCSB PDB 3SRN · PDBe 3SRN · UniProt P61823
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.