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Crystal structure of the serratia marcescens chitin-binding protein CBP21

Analyse Crystal structure of the serratia marcescens chitin-binding protein CBP21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2BEM
Type
protein
Length
510 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CBP21
UniProt
O83009
Ligands
NA, SO4
Pockets
3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CCBP21protein17014% helix, 42% strandO83009

Ligands and binding sites

  • NA · Sodium ion · metal · chains C
  • SO4 · Sulfate ion · ion · 6 copies · chains A, B, C
  • EDO · 1,2-ethanediol · additive · 15 copies · chains A, C, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11580.500.7830EDO
21380.480.7828empty
31730.450.7521empty

Interfaces

2 interfaces between chains.

  • A–C · 417 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 137 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 2BEM · Crystal structure of the Serratia marcescens chitin-binding protein CBP21 · the same entry in another collection · chain A against A, TM-score 1.00

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