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Crystal structures of SER86ASP and MET148LEU rusticyanin

Analyse Crystal structures of SER86ASP and MET148LEU rusticyanin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GY1
Type
protein
Length
308 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rusticyanin
UniProt
P24930
Ligands
CU
Pockets
1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BRusticyaninprotein1547% helix, 42% strandP24930

Ligands and binding sites

  • CU · Copper (II) ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12610.670.8331empty

Interfaces

1 interface between chains.

  • A–B · 467 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 1GY1 · Crystal structures of Ser86Asp and Met148Leu Rusticyanin · the same entry in another collection · chain A against A, TM-score 1.00

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