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Crystal structure of a putative glycosyl hydrolase with bnr repeats (REUT_B4987) from ralstonia eutropha JMP134 at 2.20 a resolution

Analyse Crystal structure of a putative glycosyl hydrolase with bnr repeats… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3B7F
Type: protein
Length: 368 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyl hydrolase, bnr repeat
UniProt: Q46R99
Ligands: CL
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycosyl hydrolase, bnr repeat	protein	368	4% helix, 41% strand	Q46R99

Ligands and binding sites

CL · Chloride ion · ion · 4 copies · chains A
EDO · 1,2-ethanediol · additive · 17 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	675	0.79	0.84	49	EDO
2	193	0.58	0.80	26	empty
3	74	0.40	0.79	24	EDO

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

3B7F · Crystal structure of a putative glycosyl hydrolase with bnr repeats (reut_b4987) from… · 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 Q46R99
Elsewhere: RCSB PDB 3B7F · PDBe 3B7F · UniProt Q46R99

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