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Crystal structure of a putative tagatose-6-phosphate KETOSE/ALDOSE isomerase (NT01CX_0292) from clostridium novyi nt at 2.35 a resolution

Analyse Crystal structure of a putative tagatose-6-phosphate KETOSE/ALDOSE isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ODP
Type: protein
Length: 392 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative tagatose-6-phosphate KETOSE/ALDOSE isomerase
UniProt: A0Q2D8
Ligands: PO4
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative tagatose-6-phosphate KETOSE/ALDOSE isomerase	protein	392	49% helix, 16% strand	A0Q2D8

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A
PG4 · Tetraethylene glycol · additive · 2 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	174	0.55	0.80	31	PO4
2	83	0.42	0.79	17	empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

3ODP · Crystal structure of a putative tagatose-6-phosphate ketose/aldose isomerase… · 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 A0Q2D8
Elsewhere: RCSB PDB 3ODP · PDBe 3ODP · UniProt A0Q2D8

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