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Structure of the global transcription regulator fapr from staphylococcus aureus

Analyse Structure of the global transcription regulator fapr from staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4A0Y
Type
protein
Length
302 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcription factor fapr
UniProt
D6UB50
Ligands
CL
Pockets
5 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscription factor faprprotein18438% helix, 34% strandD6UB50
BTranscription factor faprprotein11818% helix, 53% strandD6UB50

Ligands and binding sites

  • CL · Chloride ion · ion · 9 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1600.620.9223CL
2530.570.9017empty
3730.350.7618empty
4890.330.7314empty
5550.320.7718empty

Interfaces

1 interface between chains.

  • A–B · 1365 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 4A0Y · Structure of the global transcription regulator FapR from Staphylococcus aureus · the same entry in another collection · chain A against A, TM-score 1.00

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