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MolNFT v1 · #114343 · protein

Lnmx protein, a putative glcnac-pi de-N-acetylase from streptomyces atroolivaceus

5BMO · Putative uncharacterized protein lnmx: “Lnmx protein, a putative glcnac-pi de-N-acetylase from streptomyces atroolivaceus”. X-ray diffraction, 1 ligand (K), 4 pockets (best druggability 0.77). MolNFT v1 #114343 on GenesisL1: 3D…

PDB
5BMO
Type
protein
Length
723 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative uncharacterized protein lnmx
UniProt
Q8GGM8
Ligands
K
Pockets
4 · best druggability 0.77

Structure

x-ray diffraction · 3 distinct chains · 44% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative uncharacterized protein lnmxprotein24043% helix, 17% strandQ8GGM8
BPutative uncharacterized protein lnmxprotein24144% helix, 16% strandQ8GGM8
CPutative uncharacterized protein lnmxprotein24243% helix, 17% strandQ8GGM8

Ligands and binding sites

  • K · Potassium ion · metal · 3 copies · chains A, B, C
  • ACT · Acetate ion · additive · 3 copies · chains A, B, C

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18760.770.8060empty
26760.710.7861K, ACT
36810.690.7763ACT
46160.680.7762ACT

Interfaces

3 interfaces between chains.

  • B–C · 583 Ų buried · 11 hydrogen bonds · protein-protein
  • A–B · 573 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 565 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 5BMO · LnmX protein, a putative GlcNAc-PI de-N-acetylase from Streptomyces atroolivaceus · the same entry in another collection · chain A against A, TM-score 1.00

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