MolNFT v1 · #113395 · protein

Structures of inactive and activated dntr provide conclusive evidence for the mechanism of action of lysr transcription factors

5AE4 · Lysr-type regulatory protein: “Structures of inactive and activated dntr provide conclusive evidence for the mechanism of action of lysr…”. X-ray diffraction, 1 ligand (SCN), 3 pockets (best druggability 0.71). MolNFT v1 #113395 on…

PDB: 5AE4
Type: protein
Length: 428 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysr-type regulatory protein
UniProt: Q7WT50
Ligands: SCN
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysr-type regulatory protein	protein	215	34% helix, 27% strand	Q7WT50
B	Lysr-type regulatory protein	protein	213	34% helix, 28% strand	Q7WT50

Ligands and binding sites

SCN · Thiocyanate ion · ion · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	487	0.71	0.81	68	SCN
2	59	0.69	0.96	18	SCN
3	50	0.27	0.74	12	empty

Interfaces

1 interface between chains.

A–B · 1541 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

5AE4 · Structures of inactive and activated DntR provide conclusive evidence for the mechanism… · 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 5AE4 · PDBe 5AE4 · UniProt Q7WT50

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