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Crystal structure of a putative glycosyl hydrolase (BT2157) from bacteroides thetaiotaomicron vpi-5482 at 1.80 a resolution

Analyse Crystal structure of a putative glycosyl hydrolase (BT2157) from bacteroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OSD
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative glycosyl hydrolase
UniProt: Q8A5T1
Ligands: K
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative glycosyl hydrolase	protein	264	13% helix, 38% strand	Q8A5T1

Ligands and binding sites

K · Potassium ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 11 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	113	0.54	0.83	32	K, EDO
2	51	0.28	0.75	15	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

3OSD · Crystal structure of a putative glycosyl hydrolase (BT2157) from BACTEROIDES… · 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 Q8A5T1
Elsewhere: RCSB PDB 3OSD · PDBe 3OSD · UniProt Q8A5T1

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