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Crystal structure of RIPK1 death domain glcnacylated by epec effector nleb

Analyse Crystal structure of RIPK1 death domain glcnacylated by epec effector nleb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AC5
Type: protein
Length: 97 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Receptor-interacting SERINE/THREONINE-protein kinase 1
EC: 2.7.11.1
UniProt: Q13546
Ligands: NAG, SO4

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Receptor-interacting SERINE/THREONINE-protein kinase 1 (EC 2.7.11.1)	protein	97	71% helix, 2% strand	Q13546

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Modifications

Observed in the structure: 1 disulfide, 1 glycan (disulfide, glycosylation).

Compared structures

6AC5 · Crystal structure of RIPK1 death domain GlcNAcylated by EPEC effector NleB · the same entry in another collection · chain A against A, TM-score 1.00
Q13546 · AlphaFold monomer V2.0 prediction for receptor-interacting SERINE/THREONINE-protein… · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q13546
Elsewhere: RCSB PDB 6AC5 · PDBe 6AC5 · UniProt Q13546

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