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Streptococcus pneumoniae hyaluronate lyase W291A/W292A double mutant complex with hyaluronan hexasacchride

Analyse Streptococcus pneumoniae hyaluronate lyase W291A/W292A double mutant complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1N7Q
Type: protein
Length: 721 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hyaluronidase
EC: 4.2.2.1
Ligands: GTR, NAG, BDP
Pockets: 11 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hyaluronidase (EC 4.2.2.1)	protein	721	35% helix, 26% strand	—

Ligands and binding sites

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

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

Pockets

11 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	970	0.74	0.78	71	NAG, BDP, GTR
2	97	0.40	0.77	20	empty
3	60	0.37	0.79	18	empty
4	55	0.36	0.79	18	empty
5	68	0.35	0.77	14	empty

Compared structures

1N7Q · Streptococcus pneumoniae Hyaluronate Lyase W291A/W292A Double Mutant complex with… · 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 1N7Q · PDBe 1N7Q

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