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Crystal structure of an N-acetylgalactosamine deacetylase from F. plautii

Analyse Crystal structure of an N-acetylgalactosamine deacetylase from F. plautii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6N1A
Type: protein
Length: 386 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbohydrate-binding protein
UniProt: A0A1C7FP65
Ligands: CA, MN
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbohydrate-binding protein	protein	386	5% helix, 44% strand	A0A1C7FP65

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
MN · Manganese (II) ion · metal · 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

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	313	0.63	0.79	38	CA, GOL
2	241	0.56	0.78	30	GOL

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

6N1A · Crystal structure of an N-acetylgalactosamine deacetylase from F. plautii · 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 A0A1C7FP65
Elsewhere: RCSB PDB 6N1A · PDBe 6N1A · UniProt A0A1C7FP65

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