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X-ray crystal structure of a novel topological analogue of crambin

Analyse X-ray crystal structure of a novel topological analogue of crambin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UE7
Type: protein
Length: 92 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-crambin; Crambin
UniProt: P01542

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-crambin	protein	46	50% helix, 9% strand	—
B	Crambin	protein	46	41% helix, 13% strand	P01542

Interfaces

1 interface between chains.

A–B · 315 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 42 d-amino, 6 disulfide, 1 isopeptide (D-amino acid, disulfide, isopeptide).

Compared structures

3UE7 · X-ray crystal structure of a novel topological analogue of crambin · 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 B 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 P01542
Elsewhere: RCSB PDB 3UE7 · PDBe 3UE7 · UniProt P01542

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