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Crystal structure of bacillus subtilis codw, a non-canonical hslv-like peptidase with an impaired catalytic apparatus

Analyse Crystal structure of bacillus subtilis codw, a non-canonical hslv-like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Z3B
Type
protein
Length
2,160 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-dependent protease hslv
EC
3.4.25.-
UniProt
P39070
Ligands
NA
Pockets
20 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LATP-dependent protease hslv (EC 3.4.25.-)protein18037% helix, 27% strandP39070

Ligands and binding sites

  • NA · Sodium ion · metal · 12 copies · chains A, B, C, D, E, F, G, H, J, I, K, L

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

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111680.740.77130empty
26000.720.8081empty
34220.720.8247empty
44500.690.8062empty
53930.630.7841empty

Interfaces

19 interfaces between chains.

  • H–I · 940 Ų buried · 15 hydrogen bonds · protein-protein
  • E–F · 927 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 918 Ų buried · 13 hydrogen bonds · protein-protein
  • K–L · 912 Ų buried · 11 hydrogen bonds · protein-protein
  • C–D · 906 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 2Z3B · Crystal Structure of Bacillus Subtilis CodW, a non-canonical HslV-like peptidase with an… · the same entry in another collection · chain L against L, TM-score 1.00

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