Research workbench

Crystal structure of a trap periplasmic solute binding protein from roseobacter denitrificans, target efi-510230, with bound beta-D- glucuronate

Analyse Crystal structure of a trap periplasmic solute binding protein from roseobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OVQ
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Trap dicarboxylate ABC transporter, substrate-binding protein
UniProt: Q160Z9
Ligands: BDP, CL
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trap dicarboxylate ABC transporter, substrate-binding protein	protein	302	51% helix, 19% strand	Q160Z9

Ligands and binding sites

BDP · beta-D-glucopyranuronic acid · sugar · chains A
CL · Chloride ion · ion · 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	76	0.65	0.92	28	CL, BDP

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

4OVQ · Crystal structure of a trap periplasmic solute binding protein from roseobacter… · 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 Q160Z9
Elsewhere: RCSB PDB 4OVQ · PDBe 4OVQ · UniProt Q160Z9

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