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The crystal structure of glycosyl hydrolase from deinococcus radiodurans R1

Analyse The crystal structure of glycosyl hydrolase from deinococcus radiodurans R1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TEV
Type: protein
Length: 626 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyl hyrolase, family 3
UniProt: Q9RUP9
Pockets: 6 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycosyl hyrolase, family 3	protein	312	50% helix, 12% strand	Q9RUP9
B	Glycosyl hyrolase, family 3	protein	314	49% helix, 12% strand	Q9RUP9

Pockets

6 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	541	0.71	0.80	44	empty
2	113	0.50	0.81	18	empty
3	137	0.48	0.78	18	empty
4	164	0.46	0.76	21	empty
5	150	0.45	0.76	24	empty

Interfaces

1 interface between chains.

A–B · 727 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 modified (engineered).

Compared structures

3TEV · The crystal structure of glycosyl hydrolase from Deinococcus radiodurans R1 · 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 Q9RUP9
Elsewhere: RCSB PDB 3TEV · PDBe 3TEV · UniProt Q9RUP9

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