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Crystal structure of CSD1-CSD2 dimer I

Analyse Crystal structure of CSD1-CSD2 dimer I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5J1L
Type
protein
Length
679 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Toxr-activated gene (tage)
UniProt
O26068, O26069
Ligands
ZN
Pockets
7 · best druggability 0.57

Structure

x-ray diffraction · 4 distinct chains · 23% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AToxr-activated gene (tage)protein16027% helix, 31% strandO26068
BToxr-activated gene (tage)protein18221% helix, 31% strandO26069
CToxr-activated gene (tage)protein16223% helix, 33% strandO26068
DToxr-activated gene (tage)protein17521% helix, 30% strandO26069

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12680.570.7830empty
21290.500.8028empty
3960.490.8221empty
41780.460.7630empty
51640.450.7524empty

Interfaces

5 interfaces between chains.

  • A–B · 1351 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 1316 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 341 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 322 Ų buried · 8 hydrogen bonds · protein-protein
  • A–D · 288 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 5J1L · Crystal structure of Csd1-Csd2 dimer I · the same entry in another collection · chain A against A, TM-score 1.00

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