MolNFT v1 · #111109 · protein

RNase S in complex with stabilized S peptide

4YGW · S-peptide: ACE-lys-glu-thr-ala-ala-hcs-lys-phe-glu-hcs-gln…: “RNase S in complex with stabilized S peptide”. X-ray diffraction, 3 ligands (ACE, 4Y8, SO4). MolNFT v1 #111109 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 4YGW
Type: protein
Length: 118 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: S-peptide: ACE-lys-glu-thr-ala-ala-hcs-lys-phe-glu-hcs-gln- his-met-asp-ser; Ribonuclease…
UniProt: W0UVI3
Ligands: ACE, 4Y8, SO4

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
b	S-peptide: ACE-lys-glu-thr-ala-ala-hcs-lys-phe-glu-hcs-gln- his-met-asp-ser	protein	15	60% helix, 7% strand	—
B	Ribonuclease a C2	protein	103	17% helix, 42% strand	W0UVI3

Ligands and binding sites

ACE · Acetyl group · ligand · chains b
4Y8 · 1-hydroxypropan-2-one · ligand · chains b
SO4 · Sulfate ion · ion · 2 copies · chains b, B

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

Interfaces

1 interface between chains.

b–B · 650 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 3 covalent, 2 modified (disulfide, covalent ligand, nonstandard).

Compared structures

4YGW · RNase S in complex with stabilized S peptide · the same entry in another collection · chain b against b, 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 W0UVI3
Elsewhere: RCSB PDB 4YGW · PDBe 4YGW · UniProt W0UVI3

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