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Crystal structure of paenibacillus graminis GH74 (PGGH74)

Analyse Crystal structure of paenibacillus graminis GH74 (PGGH74) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6P2N
Type: protein
Length: 748 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xyloglucanase
UniProt: A0A089M3R3
Ligands: MG, CL
Pockets: 5 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xyloglucanase	protein	748	3% helix, 38% strand	A0A089M3R3

Ligands and binding sites

MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A

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	773	0.80	0.83	78	GOL
2	444	0.79	0.87	49	CL, MG
3	368	0.56	0.74	40	empty
4	72	0.41	0.80	18	empty
5	134	0.38	0.73	29	empty

Modifications

Observed in the structure: 19 modified (engineered).

Compared structures

6P2N · Crystal structure of Paenibacillus graminis GH74 (PgGH74) · 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 A0A089M3R3
Elsewhere: RCSB PDB 6P2N · PDBe 6P2N · UniProt A0A089M3R3

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