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Streptococcus pneumoniae hyaluronate lyase in complex with hexasaccharide hyaluronan substrate

Analyse Streptococcus pneumoniae hyaluronate lyase in complex with hexasaccharide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LOH
Type: protein
Length: 721 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hyaluronate lyase
EC: 4.2.2.1
Ligands: NAG, BDP
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hyaluronate lyase (EC 4.2.2.1)	protein	721	36% helix, 27% strand	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
BDP · beta-D-glucopyranuronic acid · sugar · 3 copies · chains A

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

Pockets

7 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	897	0.73	0.77	63	NAG, BDP
2	95	0.41	0.78	18	empty
3	147	0.40	0.73	33	empty
4	58	0.39	0.80	16	empty
5	73	0.35	0.76	17	empty

Compared structures

1LOH · Streptococcus pneumoniae Hyaluronate Lyase in Complex with Hexasaccharide Hyaluronan… · 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
Elsewhere: RCSB PDB 1LOH · PDBe 1LOH

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