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M1Q-HNTAQ1 C28S

Analyse M1Q-HNTAQ1 C28S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6KGJ
Type
protein
Length
404 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein N-terminal glutamine amidohydrolase
EC
3.5.1.122
UniProt
Q96HA8
Pockets
1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, AProtein N-terminal glutamine amidohydrolase (EC 3.5.1.122)protein20228% helix, 20% strandQ96HA8

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11140.370.7427empty

Interfaces

1 interface between chains.

  • B–A · 833 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 6KGJ · M1Q-hNTAQ1 C28S · the same entry in another collection · chain B against B, TM-score 1.00
  • Q96HA8 · AlphaFold monomer V2.0 prediction for protein N-terminal glutamine amidohydrolase (Q96HA8) · a predicted model of the same protein · chain B against A, TM-score 0.96

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