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The crystal structure of the GH30 subfamily 10 enzyme, ACXBH30A from acetivibrio clariflavus

Analyse The crystal structure of the GH30 subfamily 10 enzyme, ACXBH30A from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7N6H
Type: protein
Length: 866 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ACXBH30A
UniProt: G8LU16
Ligands: CL
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ACXBH30A	protein	433	26% helix, 30% strand	G8LU16

Ligands and binding sites

CL · Chloride ion · ion · 23 copies · chains A, B
ACT · Acetate ion · additive · 3 copies · chains A, B

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	810	0.73	0.78	72	ACT
2	68	0.39	0.78	17	empty
3	124	0.38	0.74	27	CL

Interfaces

1 interface between chains.

A–B · 395 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7N6H · The crystal structure of the GH30 subfamily 10 enzyme, AcXbh30A from Acetivibrio… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt G8LU16
Elsewhere: RCSB PDB 7N6H · PDBe 7N6H · UniProt G8LU16

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