MolNFT v1 · #125477 · protein

The mechanism by which arabinoxylanases can recognise highly decorated xylans

5LA1 · Carbohydrate binding family 6: “The mechanism by which arabinoxylanases can recognise highly decorated xylans”. X-ray diffraction, 2 ligands (XYP, CA), 3 pockets (best druggability 0.48). MolNFT v1 #125477 on GenesisL1: 3D…

PDB: 5LA1
Type: protein
Length: 474 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbohydrate binding family 6
UniProt: A0A0J9WZQ7
Ligands: XYP, CA
Pockets: 3 · best druggability 0.48

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	474	24% helix, 29% strand	A0A0J9WZQ7

Ligands and binding sites

XYP · beta-D-xylopyranose · sugar · 2 copies · chains A
CA · Calcium ion · metal · 3 copies · chains A
144 · Tris-hydroxymethyl-methyl-ammonium · additive · 3 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	137	0.48	0.78	24	144
2	86	0.46	0.81	18	XYP
3	91	0.34	0.74	17	empty

Compared structures

5LA1 · The mechanism by which arabinoxylanases can recognise highly decorated xylans · 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 A0A0J9WZQ7
Elsewhere: RCSB PDB 5LA1 · PDBe 5LA1 · UniProt A0A0J9WZQ7

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