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Crystal structure of C. elegans erh-2

Analyse Crystal structure of C. elegans erh-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7O6L
Type: protein
Length: 177 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enhancer of rudimentary homolog 2
UniProt: Q20057

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enhancer of rudimentary homolog 2	protein	91	46% helix, 27% strand	Q20057
B	Enhancer of rudimentary homolog 2	protein	86	45% helix, 29% strand	Q20057

Interfaces

1 interface between chains.

A–B · 770 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

7O6L · Crystal structure of C. elegans ERH-2 · the same entry in another collection · chain A against A, TM-score 1.00
Q20057 · AlphaFold monomer V2.0 prediction for enhancer of rudimentary homolog 2 (Q20057) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 Q20057
Elsewhere: RCSB PDB 7O6L · PDBe 7O6L · UniProt Q20057

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