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Crystal structure of amicyanin from paracoccus versutus (thiobacillus versutus)

Analyse Crystal structure of amicyanin from paracoccus versutus (thiobacillus versutus) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ID2
Type
protein
Length
318 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Amicyanin
UniProt
P22365
Ligands
CU
Pockets
2 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CAmicyaninprotein1063% helix, 44% strandP22365

Ligands and binding sites

  • CU · Copper (II) ion · metal · 3 copies · chains A, B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11240.520.8130empty
21160.400.7522empty

Interfaces

3 interfaces between chains.

  • B–C · 389 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 314 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 23 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1ID2 · Crystal structure of amicyanin from paracoccus versutus (thiobacillus versutus) · the same entry in another collection · chain A against A, TM-score 1.00
  • P22365 · AlphaFold monomer V2.0 prediction for amicyanin (P22365) · a predicted model of the same protein · chain A against A, TM-score 0.99

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