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MolNFT v1 · #156815 · protein

Crystal structure of carbon-nitrogen hydrolase from helicobacter pylori G27

6MG6: “Crystal structure of carbon-nitrogen hydrolase from helicobacter pylori G27”. X-ray diffraction, 1 ligand (SO4), 5 pockets (best druggability 0.75). MolNFT v1 #156815 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6MG6
Type
protein
Length
1,172 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Carbon-nitrogen hydrolase
UniProt
B5Z7B9
Ligands
SO4
Pockets
5 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 35% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACarbon-nitrogen hydrolaseprotein29435% helix, 28% strandB5Z7B9
B, CCarbon-nitrogen hydrolaseprotein29335% helix, 28% strandB5Z7B9
DCarbon-nitrogen hydrolaseprotein29236% helix, 28% strandB5Z7B9

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A

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

Pockets

5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12700.750.8943empty
24080.690.8155empty
33310.670.8133empty
42060.640.8328empty
53130.630.7929empty

Interfaces

6 interfaces between chains.

  • A–B · 2783 Ų buried · 50 hydrogen bonds · protein-protein
  • C–D · 2412 Ų buried · 43 hydrogen bonds · protein-protein
  • B–C · 741 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 535 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 490 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 6MG6 · Crystal structure of carbon-nitrogen hydrolase from Helicobacter pylori G27 · the same entry in another collection · chain A against A, TM-score 1.00

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