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Triclinic crystal form of inca G144A point mutant

Analyse Triclinic crystal form of inca G144A point mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6E6A
Type
protein
Length
324 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Inclusion membrane protein a
UniProt
Q50FQ0
Ligands
NA
Pockets
1 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 86% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BInclusion membrane protein aprotein16185% helix, 0% strandQ50FQ0
AInclusion membrane protein aprotein16387% helix, 0% strandQ50FQ0

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11730.440.7433empty

Interfaces

1 interface between chains.

  • B–A · 873 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 6E6A · Triclinic crystal form of IncA G144A point mutant · the same entry in another collection · chain B against B, TM-score 1.00

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