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Human DDAH-1, apo form

Analyse Human DDAH-1, apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7UT0
Type
protein
Length
566 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.68
Source
Homo sapiens
Molecule
N(G),N(G)-dimethylarginine dimethylaminohydrolase 1
EC
3.5.3.18
UniProt
O94760
Pockets
7 · best druggability 0.83

Structure

x-ray diffraction · resolution 1.68 · 2 distinct chains · 33% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AN(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (EC 3.5.3.18)protein28432% helix, 24% strandO94760
BN(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (EC 3.5.3.18)protein28233% helix, 24% strandO94760

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13760.830.9135empty
23810.820.9134empty
33650.660.8054empty
41550.570.8232empty
51690.460.7622empty

Interfaces

1 interface between chains.

  • A–B · 555 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 7UT0 · Human ddah-1, apo form · the same entry in another collection · chain A against A, TM-score 1.00
  • O94760 · AlphaFold monomer V2.0 prediction for N(G),N(G)-dimethylarginine dimethylaminohydrolase 1… · a predicted model of the same protein · chain B against A, TM-score 0.97

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