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Azurin H117G, oxidized form

Analyse Azurin H117G, oxidized form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3N2J
Type
protein
Length
1,536 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Azurin
UniProt
P00282
Ligands
CU
Pockets
15 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LAzurinprotein12815% helix, 34% strandP00282

Ligands and binding sites

  • CU · Copper (II) ion · metal · 24 copies · chains A, D, B, C, E, G, F, H, I, J, L, K

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19780.830.84124empty
26990.790.8497empty
39550.760.79120empty
41440.660.8827CU
52470.650.8339CU

Interfaces

26 interfaces between chains.

  • E–G · 375 Ų buried · 3 hydrogen bonds · protein-protein
  • E–I · 374 Ų buried · 1 hydrogen bond · protein-protein
  • C–F · 351 Ų buried · 5 hydrogen bonds · protein-protein
  • J–L · 350 Ų buried · 2 hydrogen bonds · protein-protein
  • H–J · 350 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

  • 3N2J · Azurin H117G, oxidized form · the same entry in another collection · chain L against L, TM-score 1.00

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