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MolNFT v1 · #177745 · protein

Crystal structure of a L-rhamnose-alpha-1,4-D-glucuronate lyase from fusarium oxysporum 12S, L-rha complex

7ESM: “Crystal structure of a L-rhamnose-alpha-1,4-D-glucuronate lyase from fusarium oxysporum 12S, L-rha complex”. X-ray diffraction, 5 ligands (NAG, BMA, MAN), 2 pockets (best druggability 0.73). MolNFT v1 #177745 on GenesisL1: 3D…

PDB
7ESM
Type
protein
Length
419 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-rhamnose-alpha-1,4-D-glucuronate lyase
EC
4.2.2.-
Ligands
NAG, BMA, MAN, RAM, NA
Pockets
2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AL-rhamnose-alpha-1,4-D-glucuronate lyase (EC 4.2.2.-)protein4195% helix, 47% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • BMA · beta-D-mannopyranose · sugar
  • MAN · alpha-D-mannopyranose · sugar
  • RAM · alpha-L-rhamnopyranose · sugar · chains A
  • NA · Sodium ion · metal · chains A
  • ACT · Acetate ion · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13000.730.8649empty
21790.470.7623RAM

Modifications

Observed in the structure: 1 glycan (N-glycosylation).

Compared structures

  • 7ESM · Crystal structure of a L-rhamnose-alpha-1,4-D-glucuronate lyase from Fusarium oxysporum… · the same entry in another collection · chain A against A, TM-score 1.00

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