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C-terminal CBM35 from amycolatopsis orientalis exo-chitosanase csxa in complex with digalacturonic acid

Analyse C-terminal CBM35 from amycolatopsis orientalis exo-chitosanase csxa in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VZQ
Type: protein
Length: 252 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Exo-beta-D-glucosaminidase
UniProt: Q56F26
Ligands: GTR, AQA, CA, NA

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Exo-beta-D-glucosaminidase	protein	126	2% helix, 54% strand	Q56F26

Ligands and binding sites

GTR · beta-D-galactopyranuronic acid · ligand · 2 copies · chains A, B
AQA · 4-deoxy-beta-L-threo-hex-4-enopyranuronic acid · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · 4 copies · chains A, B
NA · Sodium ion · metal · chains B
EDO · 1,2-ethanediol · additive · 5 copies · chains A, B

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

Compared structures

2VZQ · C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
Q56F26 · AlphaFold monomer V2.0 prediction for exo-beta-D-glucosaminidase (Q56F26) · a predicted model of the same protein · chain B 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 Q56F26
Elsewhere: RCSB PDB 2VZQ · PDBe 2VZQ · UniProt Q56F26

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