GL1X · GenesisL1 explorer

Research workbench

Crystallographic structures of ribonuclease S variants with nonpolar substitution at position 13: packing and cavities

Analyse Crystallographic structures of ribonuclease S variants with nonpolar… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1RBH
Type
protein
Length
119 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribonuclease S (S-peptide); Ribonuclease S (S-protein)
EC
3.1.27.5
UniProt
P61823
Ligands
NH2, SO4

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
SRibonuclease S (S-peptide)protein1560% helix, 7% strandP61823
ARibonuclease S (S-protein) (EC 3.1.27.5)protein10416% helix, 41% strandP61823

Ligands and binding sites

  • NH2 · Amino group · ion · chains S
  • SO4 · Sulfate ion · ion · chains S, A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • S–A · 701 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1RBH · Crystallographic structures of ribonuclease S variants with nonpolar substitution at… · the same entry in another collection · chain S against S, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.