MolNFT v1 · #120120 · protein

Crystal structure of chitinase-H from O. furnacalis in complex with chitohepatose

5GQB: “Crystal structure of chitinase-H from O. furnacalis in complex with chitohepatose”. X-ray diffraction, 2 ligands (GCS, NAG), 2 pockets (best druggability 0.70). MolNFT v1 #120120 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 5GQB
Type: protein
Length: 538 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitinase
UniProt: Q4AE59
Ligands: GCS, NAG
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitinase	protein	538	28% helix, 26% strand	Q4AE59

Ligands and binding sites

GCS · 2-amino-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A

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

Pockets

2 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	527	0.70	0.79	53	GCS
2	107	0.35	0.73	22	empty

Modifications

Observed in the structure: 2 glycan, 1 disulfide (N-glycosylation, disulfide).

Compared structures

5GQB · Crystal structure of chitinase-h from O. furnacalis in complex with chitohepatose · 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 Q4AE59
Elsewhere: RCSB PDB 5GQB · PDBe 5GQB · UniProt Q4AE59

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