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Solution structure of rrm domain in PARP14

Analyse Solution structure of rrm domain in PARP14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1X5P
Type: protein
Length: 97 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Negative elongation factor E
UniProt: P18615

Structure

solution nmr · 1 distinct chain · 19% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Negative elongation factor E	protein	97	19% helix, 28% strand	P18615

Compared structures

1X5P · Solution structure of RRM domain in Parp14 · the same entry in another collection · chain A against A, TM-score 1.00
P18615 · AlphaFold monomer V2.0 prediction for negative elongation factor E (P18615) · a predicted model of the same protein · chain A against A, TM-score 0.76

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 P18615
Elsewhere: RCSB PDB 1X5P · PDBe 1X5P · UniProt P18615

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