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D192N mutant of rhamnogalacturonan acetylesterase

Analyse D192N mutant of rhamnogalacturonan acetylesterase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3C1U
Type: protein
Length: 231 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rhamnogalacturonan acetylesterase
EC: 3.1.1.-
UniProt: Q00017
Ligands: NAG

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rhamnogalacturonan acetylesterase (EC 3.1.1.-)	protein	231	39% helix, 16% strand	Q00017

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
ACT · Acetate ion · additive · chains A

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

Modifications

Observed in the structure: 2 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

3C1U · D192N mutant of Rhamnogalacturonan acetylesterase · the same entry in another collection · chain A against A, TM-score 1.00
Q00017 · AlphaFold monomer V2.0 prediction for rhamnogalacturonan acetylesterase (Q00017) · 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 Q00017
Elsewhere: RCSB PDB 3C1U · PDBe 3C1U · UniProt Q00017

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