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Structure of CTGH5-CBM6, an arabinoxylan-specific xylanase.

Analyse Structure of CTGH5-CBM6, an arabinoxylan-specific xylanase. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Y8K
Type: protein
Length: 480 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbohydrate binding family 6
UniProt: A3DHG6
Ligands: NA, CA
Pockets: 4 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbohydrate binding family 6	protein	480	24% helix, 29% strand	A3DHG6

Ligands and binding sites

NA · Sodium ion · metal · 4 copies · chains A
CA · Calcium ion · metal · chains A
GOL · Glycerol · additive · 8 copies · chains A

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

Pockets

4 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	123	0.51	0.80	27	GOL
2	113	0.45	0.78	20	empty
3	149	0.41	0.74	27	GOL
4	55	0.35	0.79	12	empty

Compared structures

2Y8K · Structure of CtGH5-CBM6, an arabinoxylan-specific xylanase. · 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 A3DHG6
Elsewhere: RCSB PDB 2Y8K · PDBe 2Y8K · UniProt A3DHG6

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