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Structure of a streptococcus pneumoniae family 85 glycoside hydrolase, endo-D.

Analyse Structure of a streptococcus pneumoniae family 85 glycoside hydrolase, endo-D. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W91
Type: protein
Length: 635 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-N-acetylglucosaminidase D
UniProt: Q93HW0
Pockets: 5 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-N-acetylglucosaminidase D	protein	635	20% helix, 36% strand	Q93HW0

Ligands and binding sites

1PE · Pentaethylene glycol · additive · chains A

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

Pockets

5 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	199	0.66	0.85	33	empty
2	139	0.47	0.78	28	empty
3	101	0.42	0.77	17	empty
4	84	0.40	0.78	23	empty
5	58	0.31	0.76	15	empty

Compared structures

2W91 · Structure of a Streptococcus pneumoniae family 85 glycoside hydrolase, Endo-D. · 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 Q93HW0
Elsewhere: RCSB PDB 2W91 · PDBe 2W91 · UniProt Q93HW0

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