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Crambin at ultra-high resolution: valence electron density.

Analyse Crambin at ultra-high resolution: valence electron density. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EJG
Type: protein
Length: 46 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Crambin (PRO22,SER22/LEU25,ILE25)
UniProt: P01542

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Crambin (PRO22,SER22/LEU25,ILE25)	protein	46	41% helix, 9% strand	P01542

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1EJG · Crambin at ultra-high resolution: valence electron density. · the same entry in another collection · chain A against A, TM-score 1.00
P01542 · AlphaFold monomer V2.0 prediction for crambin (P01542) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P01542
Elsewhere: RCSB PDB 1EJG · PDBe 1EJG · UniProt P01542

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