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Crystal structure of se-met fucosyltransferase nodz from bradyrhizobium

Analyse Crystal structure of se-met fucosyltransferase nodz from bradyrhizobium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OCX
Type: protein
Length: 292 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nodulation fucosyltransferase nodz
EC: 2.4.1.-
UniProt: Q9AQ17
Ligands: PO4
Pockets: 4 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nodulation fucosyltransferase nodz (EC 2.4.1.-)	protein	292	44% helix, 20% strand	Q9AQ17

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	183	0.45	0.74	32	empty
2	99	0.39	0.75	18	empty
3	69	0.31	0.74	13	empty
4	54	0.29	0.75	19	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

2OCX · Crystal structure of Se-Met fucosyltransferase NodZ from Bradyrhizobium · 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 Q9AQ17
Elsewhere: RCSB PDB 2OCX · PDBe 2OCX · UniProt Q9AQ17

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