MolNFT v1 · #153320 · protein

Crystal structure of ostrinia furnacalis group II chitinase catalytic domain 1 in complex with a napthalimide derivative

6JAW: “Crystal structure of ostrinia furnacalis group II chitinase catalytic domain 1 in complex with a napthalimide…”. X-ray diffraction, 2 ligands (BBO, NAG), 1 pocket (best druggability 0.65). MolNFT v1 #153320 on GenesisL1: 3D…

PDB: 6JAW
Type: protein
Length: 377 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Group II chitinase
EC: 3.2.1.14
UniProt: A0A221ZS22
Ligands: BBO, NAG
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Group II chitinase (EC 3.2.1.14)	protein	377	37% helix, 21% strand	A0A221ZS22

Ligands and binding sites

BBO · 2-[3-(morpholin-4-yl)propyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione · ligand · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 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	405	0.65	0.78	44	BBO

Modifications

Observed in the structure: 3 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

6JAW · Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex… · 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 A0A221ZS22
Elsewhere: RCSB PDB 6JAW · PDBe 6JAW · UniProt A0A221ZS22

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