MolNFT v1 · #50551 · protein
Thermodynamic and structural consequences of changing a sulphur atom to a methylene group in the M13NLE mutation in ribonuclease S
2RLN: “Thermodynamic and structural consequences of changing a sulphur atom to a methylene group in the M13NLE…”. X-ray diffraction, 2 ligands (NH2, SO4). MolNFT v1 #50551 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2RLN
- Type
- protein
- Length
- 119 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease; Ribonuclease S (S-protein)
- EC
- 3.1.27.5
- UniProt
- P00656
- Ligands
- NH2, SO4
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| S | Ribonuclease | protein | 15 | 60% helix, 7% strand | — |
| E | Ribonuclease S (S-protein) (EC 3.1.27.5) | protein | 104 | 16% helix, 41% strand | P00656 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- S–E · 705 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 1 modified (disulfide, nonstandard).
Compared structures
- 2RLN · Thermodynamic and structural consequences of changing a sulphur atom to a methylene group… · the same entry in another collection · chain S against S, 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 P00656
- Elsewhere: RCSB PDB 2RLN · PDBe 2RLN · UniProt P00656
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.