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Structure and metal-loading of a soluble periplasm cupro-protein: zn- cuca-closed (semet)

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

PDB
2XL9
Type
protein
Length
466 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SLL1785 protein
UniProt
P73600
Ligands
TAM, ZN
Pockets
2 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASLL1785 proteinprotein23118% helix, 35% strandP73600
BSLL1785 proteinprotein23519% helix, 34% strandP73600

Ligands and binding sites

  • TAM · Tris(hydroxyethyl)aminomethane · ligand · chains A
  • ZN · Zinc ion · metal · 3 copies · chains A, B

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
16460.750.8155empty
2690.410.8016empty

Interfaces

1 interface between chains.

  • A–B · 927 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified, 2 disulfide (engineered, disulfide).

Compared structures

  • 2XL9 · Structure and metal-loading of a soluble periplasm cupro-protein: Zn- CucA-closed (SeMet) · the same entry in another collection · chain A against A, TM-score 1.00

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