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Crystal structure of a novel 4-O-alpha-L-rhamnosyl-beta-D- glucuronidase from fusarium oxysporum 12S, ligand-free form

Analyse Crystal structure of a novel 4-O-alpha-L-rhamnosyl-beta-D- glucuronidase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DFQ
Type: protein
Length: 457 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-O-alpha-L-rhamnosyl-beta-D-glucuronidase
EC: 3.2.1.31
Ligands: NAG
Pockets: 3 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-O-alpha-L-rhamnosyl-beta-D-glucuronidase (EC 3.2.1.31)	protein	457	32% helix, 27% strand	—

Ligands and binding sites

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

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	163	0.48	0.77	25	empty
2	102	0.47	0.80	24	empty
3	56	0.29	0.74	16	empty

Modifications

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

Compared structures

7DFQ · Crystal Structure of a novel 4-O-alpha-L-rhamnosyl-beta-D-glucuronidase from Fusarium… · 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
Elsewhere: RCSB PDB 7DFQ · PDBe 7DFQ

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