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Structure of the D169N mutant of C. immitis chitinase 1

Analyse Structure of the D169N mutant of C. immitis chitinase 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LL6
Type: protein
Length: 1,568 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitinase 1
EC: 3.2.1.14
UniProt: P54196
Pockets: 11 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Chitinase 1 (EC 3.2.1.14)	protein	392	35% helix, 21% strand	P54196

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1141	0.83	0.84	142	empty
2	1172	0.83	0.84	135	empty
3	767	0.73	0.79	93	empty
4	473	0.67	0.78	54	empty
5	80	0.49	0.83	25	empty

Interfaces

5 interfaces between chains.

A–B · 785 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 781 Å² buried · 11 hydrogen bonds · protein-protein
B–C · 392 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 362 Å² buried · 4 hydrogen bonds · protein-protein
B–D · 88 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1LL6 · Structure of the D169N mutant of C. immitis chitinase 1 · 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 P54196
Elsewhere: RCSB PDB 1LL6 · PDBe 1LL6 · UniProt P54196

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