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MolNFT v1 · #123911 · protein

ASPARTYL/ASPARAGINYL beta-hydroxylase (ASPH)OXYGENASE and tpr domains in complex with manganese and N-oxalylglycine

5JZA: “ASPARTYL/ASPARAGINYL beta-hydroxylase (ASPH)OXYGENASE and tpr domains in complex with manganese and…”. X-ray diffraction, 2 ligands (OGA, MN), 1 pocket (best druggability 0.64). MolNFT v1 #123911 on GenesisL1: 3D structure, binding…

PDB
5JZA
Type
protein
Length
429 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ASPARTYL/ASPARAGINYL beta-hydroxylase
EC
1.14.11.16
UniProt
Q12797
Ligands
OGA, MN
Pockets
1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AASPARTYL/ASPARAGINYL beta-hydroxylase (EC 1.14.11.16)protein42952% helix, 16% strandQ12797

Ligands and binding sites

  • OGA · N-oxalylglycine · ligand · chains A
  • MN · Manganese (II) ion · metal · chains A
  • GOL · Glycerol · additive · 4 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12990.640.8147MN, OGA

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 5JZA · Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q12797 · AlphaFold monomer V2.0 prediction for ASPARTYL/ASPARAGINYL beta- hydroxylase (Q12797) · a predicted model of the same protein · chain A against A, TM-score 0.92

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