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Crystal structure of the csce with ligand to have a insight into the catalytic mechanism

Analyse Crystal structure of the csce with ligand to have a insight into the catalytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7D5G
Type: protein
Length: 389 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellobiose 2-epimerase
EC: 5.1.3.11
UniProt: A4XGA6
Ligands: FRU, BGC, CL
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellobiose 2-epimerase (EC 5.1.3.11)	protein	389	54% helix, 13% strand	A4XGA6

Ligands and binding sites

FRU · beta-D-fructofuranose · sugar · chains A
BGC · beta-D-glucopyranose · sugar · chains A
CL · Chloride ion · ion · 3 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	303	0.66	0.81	33	FRU, BGC
2	114	0.55	0.83	25	empty

Compared structures

7D5G · Crystal structure of the CsCE with ligand to have a insight into the catalytic mechanism · the same entry in another collection · 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 A4XGA6
Elsewhere: RCSB PDB 7D5G · PDBe 7D5G · UniProt A4XGA6

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