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Crystal structure of carbohydrate esterase pbeacxe, in complex with meglcpa-xylp

Analyse Crystal structure of carbohydrate esterase pbeacxe, in complex with meglcpa-xylp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TOH
Type: protein
Length: 379 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sgnh hydrolase
UniProt: A0A5M4AV20
Ligands: GCV, XYP
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sgnh hydrolase	protein	379	26% helix, 32% strand	A0A5M4AV20

Ligands and binding sites

GCV · 4-O-methyl-alpha-D-glucopyranuronic acid · ligand · chains A
XYP · beta-D-xylopyranose · sugar · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	54	0.72	0.99	22	empty
2	71	0.36	0.77	23	XYP, GCV
3	74	0.35	0.76	19	empty
4	69	0.32	0.75	17	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

7TOH · Crystal structure of carbohydrate esterase PbeAcXE, in complex with MeGlcpA-Xylp · 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 A0A5M4AV20
Elsewhere: RCSB PDB 7TOH · PDBe 7TOH · UniProt A0A5M4AV20

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