Research workbench

C. elegans CLP1 bound to AMP-pnp, and MG2+

Analyse C. elegans CLP1 bound to AMP-pnp, and MG2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OHV
Type: protein
Length: 396 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P52874

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	396	—	P52874

Compared structures

4OHV · C. Elegans Clp1 bound to AMP-PNP, and Mg2+ · the same entry in another collection · chain A against A, TM-score 1.00
P52874 · AlphaFold monomer V2.0 prediction for protein clpf-1 (P52874) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P52874
Elsewhere: RCSB PDB 4OHV · PDBe 4OHV · UniProt P52874

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