MolNFT v1 · #120575 · protein

The complex of glycoside hydrolase 5 lichenase from caldicellulosiruptor sp. F32 E188Q mutant and cellotetraose

5H4R · Beta-1,3-1,4-glucanase: “The complex of glycoside hydrolase 5 lichenase from caldicellulosiruptor sp. F32 E188Q mutant and…”. X-ray diffraction, 1 ligand (BGC), 1 pocket (best druggability 0.51). MolNFT v1 #120575 on GenesisL1: 3D…

PDB: 5H4R
Type: protein
Length: 375 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-1,3-1,4-glucanase
UniProt: R9RX81
Ligands: BGC
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-1,3-1,4-glucanase	protein	375	40% helix, 13% strand	R9RX81

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 4 copies · chains A
GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	225	0.51	0.76	26	BGC, GOL

Compared structures

5H4R · the complex of Glycoside Hydrolase 5 Lichenase from Caldicellulosiruptor sp. F32 E188Q… · 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 R9RX81
Elsewhere: RCSB PDB 5H4R · PDBe 5H4R · UniProt R9RX81

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