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POA1P S30A mutant in complex with ADP-ribose

Analyse POA1P S30A mutant in complex with ADP-ribose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LFT
Type: protein
Length: 166 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P38218
Ligands: APR

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	166	—	P38218

Ligands and binding sites

APR · Adenosine-5-diphosphoribose · ligand · chains A
ACT · Acetate ion · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6LFT · Poa1p S30A mutant in complex with ADP-ribose · the same entry in another collection · chain A against A, TM-score 1.00
P38218 · AlphaFold monomer V2.0 prediction for ADP-ribose 1''-phosphate phosphatase (P38218) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P38218
Elsewhere: RCSB PDB 6LFT · PDBe 6LFT · UniProt P38218

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