MolNFT v1 · #8213 · protein

Hinge-bending motion of D-allose binding protein from escherichia COLI: three open conformations

1GUB · D-allose-binding periplasmic protein: “Hinge-bending motion of D-allose binding protein from escherichia COLI: three open conformations”. X-ray diffraction, 1 ligand (NI), 1 pocket (best druggability 0.54). MolNFT v1 #8213 on…

PDB: 1GUB
Type: protein
Length: 288 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-allose-binding periplasmic protein
UniProt: P39265
Ligands: NI
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-allose-binding periplasmic protein	protein	288	46% helix, 22% strand	P39265

Ligands and binding sites

NI · Nickel (II) ion · metal · 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	281	0.54	0.76	32	empty

Compared structures

1GUB · Hinge-bending motion of D-allose binding protein from Escherichia coli: three open… · the same entry in another collection · chain A against A, TM-score 1.00
P39265 · AlphaFold monomer V2.0 prediction for D-allose-binding periplasmic protein (P39265) · a predicted model of the same protein · chain A against A, TM-score 0.82

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 P39265
Elsewhere: RCSB PDB 1GUB · PDBe 1GUB · UniProt P39265

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.