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Crystal structure of ST0689, an archaeal hepn homologue

Analyse Crystal structure of ST0689, an archaeal hepn homologue in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WOL
Type: protein
Length: 122 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 122AA long conserved hypothetical protein
UniProt: Q974G3
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	122AA long conserved hypothetical protein	protein	122	67% helix, 0% strand	Q974G3

Ligands and binding sites

TBU · Tertiary-butyl alcohol · additive · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	97	0.40	0.76	20	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1WOL · Crystal Structure of ST0689, an archaeal HEPN homologue · 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 Q974G3
Elsewhere: RCSB PDB 1WOL · PDBe 1WOL · UniProt Q974G3

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