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Crystal structure of S.CUEP

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

PDB
4GQZ
Type
protein
Length
636 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative periplasmic or exported protein
UniProt
Q8ZL99
Ligands
CL
Pockets
2 · best druggability 0.47

Structure

x-ray diffraction · 3 distinct chains · 11% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative periplasmic or exported proteinprotein15611% helix, 45% strandQ8ZL99
B, CPutative periplasmic or exported proteinprotein16111% helix, 42% strandQ8ZL99
DPutative periplasmic or exported proteinprotein15811% helix, 46% strandQ8ZL99

Ligands and binding sites

  • CL · Chloride ion · ion · 2 copies · chains A, B, C, D

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11400.470.7827empty
21360.410.7522empty

Interfaces

4 interfaces between chains.

  • C–D · 1074 Ų buried · 28 hydrogen bonds · protein-protein
  • A–B · 1025 Ų buried · 21 hydrogen bonds · protein-protein
  • A–C · 253 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 245 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 19 modified, 4 disulfide (engineered, disulfide, oxidation).

Compared structures

  • 4GQZ · Crystal Structure of S.CueP · the same entry in another collection · chain A against A, TM-score 1.00

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