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Crystal structure of a putative alpha-L-fucosidase (BACOVA_04357) from bacteroides ovatus atcc 8483 at 1.59 a resolution

Analyse Crystal structure of a putative alpha-L-fucosidase (BACOVA_04357) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZRX
Type: protein
Length: 581 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: F5/8 type C domain protein
UniProt: A7M2M0
Pockets: 3 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	F5/8 type C domain protein	protein	581	24% helix, 32% strand	A7M2M0

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 7 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	131	0.48	0.78	30	EDO
2	87	0.34	0.74	15	EDO
3	50	0.25	0.73	13	empty

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

4ZRX · Crystal structure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A7M2M0
Elsewhere: RCSB PDB 4ZRX · PDBe 4ZRX · UniProt A7M2M0

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