Research workbench

[I11G]HYEN D

Analyse [I11G]HYEN D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7RIJ
Type: protein
Length: 60 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: C0HLN8

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	30	—	C0HLN8
B	—	protein	30	—	—

Ligands and binding sites

ACT · Acetate ion · additive · 3 copies · chains A, B

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

Compared structures

7RIJ · [I11G]hyen D · the same entry in another collection · chain A against A, TM-score 1.00
C0HLN8 · AlphaFold monomer V2.0 prediction for cyclotide hyen-D (C0HLN8) · a predicted model of the same protein · chain A against A, TM-score 0.84

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 C0HLN8
Elsewhere: RCSB PDB 7RIJ · PDBe 7RIJ · UniProt C0HLN8

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