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Crystal structure of M1 zinc metallopeptidase E323A mutant from deinococcus radiodurans

Analyse Crystal structure of M1 zinc metallopeptidase E323A mutant from deinococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6IFF
Type
protein
Length
858 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Zinc metalloprotease
UniProt
Q9RVZ5
Ligands
TYR, ZN, NA
Pockets
7 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BZinc metalloproteaseprotein42929% helix, 34% strandQ9RVZ5

Ligands and binding sites

  • TYR · Tyrosine · ligand · 2 copies · chains A, B
  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • NA · Sodium ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12300.630.8228TYR
22040.590.8128TYR
3570.430.8315empty
4670.390.7924empty
5920.360.7523empty

Interfaces

1 interface between chains.

  • A–B · 412 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 6IFF · Crystal structure of M1 zinc metallopeptidase E323A mutant from Deinococcus radiodurans · the same entry in another collection · chain B against B, TM-score 1.00

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