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Endo-beta-1,2-glucanase from chitinophaga pinensis - ligand free form

Analyse Endo-beta-1,2-glucanase from chitinophaga pinensis - ligand free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GZH
Type: protein
Length: 852 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-1,2-glucanase
UniProt: C7PIC2
Ligands: GLC, IOD
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Endo-beta-1,2-glucanase	protein	426	44% helix, 14% strand	C7PIC2

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B
IOD · Iodide ion · ion · 24 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1144	0.79	0.81	93	empty
2	251	0.54	0.76	30	IOD
3	217	0.51	0.76	34	IOD
4	157	0.44	0.75	22	empty
5	128	0.41	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 1204 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

5GZH · Endo-beta-1,2-glucanase from Chitinophaga pinensis - ligand free form · 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 C7PIC2
Elsewhere: RCSB PDB 5GZH · PDBe 5GZH · UniProt C7PIC2

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