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Native bacteroidetes-affiliated GH5 cellulase linked with a polysaccharide utilization locus

Analyse Native bacteroidetes-affiliated GH5 cellulase linked with a polysaccharide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4YHG
Type: protein
Length: 750 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GH5
EC: 3.2.1.4
UniProt: A0A076MPD7
Ligands: BGC
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GH5 (EC 3.2.1.4)	protein	389	42% helix, 13% strand	A0A076MPD7
B	GH5 (EC 3.2.1.4)	protein	361	44% helix, 12% strand	A0A076MPD7

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 3 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	786	0.76	0.80	64	empty
2	385	0.64	0.78	32	BGC
3	197	0.48	0.75	25	empty

Interfaces

1 interface between chains.

A–B · 656 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

4YHG · Native bacteroidetes-affiliated GH5 cellulase linked with a polysaccharide utilization… · the same entry in another collection · chain B against B, 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 A0A076MPD7
Elsewhere: RCSB PDB 4YHG · PDBe 4YHG · UniProt A0A076MPD7

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