GL1X · GenesisL1 explorer

MolNFT v1 · #142741 · protein

Ldcorocc double mutant- I486A-L493A

6ADZ · Coronin-like protein: “Ldcorocc double mutant- I486A-L493A”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.37). MolNFT v1 #142741 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6ADZ
Type
protein
Length
193 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Coronin-like protein
UniProt
Q3T1U8
Ligands
SO4
Pockets
1 · best druggability 0.37

Structure

x-ray diffraction · 4 distinct chains · 93% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACoronin-like proteinprotein4892% helix, 0% strandQ3T1U8
CCoronin-like proteinprotein4894% helix, 0% strandQ3T1U8
BCoronin-like proteinprotein5194% helix, 0% strandQ3T1U8
DCoronin-like proteinprotein4691% helix, 0% strandQ3T1U8

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A, D, C, 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
1910.370.7518empty

Interfaces

6 interfaces between chains.

  • A–B · 1024 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 897 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 850 Ų buried · 0 hydrogen bonds · protein-protein
  • C–B · 675 Ų buried · 11 hydrogen bonds · protein-protein
  • B–D · 227 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6ADZ · LdCoroCC Double mutant- I486A-L493A · the same entry in another collection · chain A against A, TM-score 1.00

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