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Structure and metal-loading of a soluble periplasm cupro-protein: cu- cuca-closed

Analyse Structure and metal-loading of a soluble periplasm cupro-protein: cu… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2XLA
Type
protein
Length
936 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SLL1785 protein
UniProt
P73600
Ligands
URE, CU
Pockets
4 · best druggability 0.74

Structure

x-ray diffraction · 3 distinct chains · 18% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASLL1785 proteinprotein23318% helix, 34% strandP73600
B, DSLL1785 proteinprotein23418% helix, 35% strandP73600
CSLL1785 proteinprotein23517% helix, 35% strandP73600

Ligands and binding sites

  • URE · Urea · ligand · 4 copies · chains A, B, C, D
  • CU · Copper (II) ion · metal · 4 copies · chains A, B, C, D

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16740.740.8055empty
25810.740.8150empty
35180.630.7545empty
41150.370.7422empty

Interfaces

3 interfaces between chains.

  • A–B · 873 Ų buried · 17 hydrogen bonds · protein-protein
  • C–D · 857 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 316 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 2XLA · Structure and metal-loading of a soluble periplasm cupro-protein: Cu- CucA-closed · the same entry in another collection · chain A against A, TM-score 1.00

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