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Crystal structure of ntf-2 like protein of unknown function (YP_553245.1) from burkholderia xenovorans LB400 at 1.85 a resolution

Analyse Crystal structure of ntf-2 like protein of unknown function (YP_553245.1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EN8
Type: protein
Length: 128 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized ntf-2 like protein
UniProt: Q13PU4
Ligands: CA
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized ntf-2 like protein	protein	128	30% helix, 43% strand	Q13PU4

Ligands and binding sites

CA · Calcium ion · metal · chains A
ACT · Acetate ion · additive · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A
PG4 · Tetraethylene glycol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	133	0.56	0.83	29	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

3EN8 · Crystal structure of NTF-2 like protein of unknown function (YP_553245.1) from… · 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 Q13PU4
Elsewhere: RCSB PDB 3EN8 · PDBe 3EN8 · UniProt Q13PU4

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