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Crystal structure analysis of the arsr homologue DNA-binding protein from P. horikoshii OT3

Analyse Crystal structure analysis of the arsr homologue DNA-binding protein from P.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ULY
Type: protein
Length: 190 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein PH1932
UniProt: O59595
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein PH1932	protein	190	63% helix, 14% strand	O59595

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	358	0.57	0.75	34	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

1ULY · Crystal structure analysis of the ArsR homologue DNA-binding protein from P. horikoshii… · 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 O59595
Elsewhere: RCSB PDB 1ULY · PDBe 1ULY · UniProt O59595

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