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The Crystal Structure of the C-terminal Domain of Aquifex aeolicus PilT

Analyse The Crystal Structure of the C-terminal Domain of Aquifex aeolicus PilT in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2EYU
Type: protein
Length: 494 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.87
Source: Aquifex aeolicus
Molecule: twitching motility protein PilT
Ligands: SO4
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · resolution 1.87 · 1 distinct chain · 47% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	twitching motility protein PilT	protein	247	47% helix, 20% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · chains 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	401	0.57	0.74	38	empty
2	285	0.51	0.74	34	SO4
3	61	0.30	0.75	12	empty

Interfaces

1 interface between chains.

A–B · 204 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

2EYU · The crystal structure of the C-terminal domain of aquifex aeolicus pilt · 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
Elsewhere: RCSB PDB 2EYU · PDBe 2EYU

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