MolNFT v1 · #24378 · protein

Dntr from burkholderia sp. strain dnt

1UTB · Lysr-type regulatory protein: “Dntr from burkholderia sp. strain dnt”. X-ray diffraction, 3 pockets (best druggability 0.72). MolNFT v1 #24378 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1UTB
Type: protein
Length: 441 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysr-type regulatory protein
UniProt: Q7WT50
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysr-type regulatory protein	protein	214	36% helix, 27% strand	Q7WT50
B	Lysr-type regulatory protein	protein	227	37% helix, 26% strand	Q7WT50

Ligands and binding sites

GOL · Glycerol · additive · 5 copies · chains A, B
ACT · Acetate ion · additive · 2 copies · chains A, B

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

Pockets

3 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	421	0.72	0.82	78	GOL, ACT
2	52	0.44	0.84	16	empty
3	53	0.33	0.78	14	GOL

Interfaces

1 interface between chains.

A–B · 1563 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

1UTB · DntR from Burkholderia sp. strain DNT · 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 Q7WT50
Elsewhere: RCSB PDB 1UTB · PDBe 1UTB · UniProt Q7WT50

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