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Structure of chitinase D from serratia proteamaculans revealed an unusually constrained substrate binding site

Analyse Structure of chitinase D from serratia proteamaculans revealed an unusually… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LGX
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
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase family 18 (EC 3.2.1.14)	protein	398	37% helix, 20% strand	A8GFD6

Ligands and binding sites

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	325	0.66	0.81	39	ACT, GOL
2	100	0.43	0.78	22	GOL
3	68	0.31	0.74	15	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

4LGX · Structure of Chitinase D from Serratia proteamaculans revealed an unusually constrained… · 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 4LGX · PDBe 4LGX · UniProt A8GFD6

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