MolNFT v1 · #103868 · protein

Crystal structure of chitinase D from serratia proteamaculans in complex with N-acetyl glucosamine, a hydrolyzed product of hexasaccharide at 1.7 ångström resolution

4PTM · Glycoside hydrolase family 18: “Crystal structure of chitinase D from serratia proteamaculans in complex with N-acetyl glucosamine, a…”. X-ray diffraction, 1 ligand (NAG), 3 pockets (best druggability 0.68). MolNFT v1 #103868 on…

PDB: 4PTM
Type: protein
Length: 398 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase family 18
EC: 3.2.1.14
UniProt: A8GFD6
Ligands: NAG
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase family 18 (EC 3.2.1.14)	protein	398	38% helix, 20% strand	A8GFD6

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
GOL · Glycerol · additive · 2 copies · chains A
ACT · Acetate ion · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	309	0.68	0.82	33	ACT, NAG, GOL
2	87	0.39	0.77	22	GOL
3	54	0.33	0.78	18	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

4PTM · Crystal Structure of Chitinase D from Serratia proteamaculans in complex with N-acetyl… · 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 A8GFD6
Elsewhere: RCSB PDB 4PTM · PDBe 4PTM · UniProt A8GFD6

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