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Crystal structure of citrus MAF1 in space group P 31 2 1

Analyse Crystal structure of citrus MAF1 in space group P 31 2 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5U4Z
Type
protein
Length
358 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Repressor of RNA polymerase III transcription
UniProt
G9I821
Ligands
SO4
Pockets
4 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARepressor of RNA polymerase III transcriptionprotein18146% helix, 24% strandG9I821
BRepressor of RNA polymerase III transcriptionprotein17747% helix, 23% strandG9I821

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11720.520.7924empty
2900.480.8219SO4
3910.370.7617SO4
4550.330.7817empty

Interfaces

1 interface between chains.

  • A–B · 679 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 5U4Z · Crystal structure of citrus MAF1 in space group P 31 2 1 · the same entry in another collection · chain A against A, TM-score 1.00

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