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Crystal structure of the SAMD1 SAM domain in another crystal form

Analyse Crystal structure of the SAMD1 SAM domain in another crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LUK
Type
protein
Length
1,380 residues
Chains
20
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Atherin
UniProt
Q6SPF0
Ligands
SO4
Pockets
16 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, TAtherinprotein6971% helix, 0% strandQ6SPF0

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 18 copies · chains A, B, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T

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

Pockets

16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17090.780.8369empty
27010.780.8365empty
32280.650.8427empty
42050.630.8324empty
52030.630.8325empty

Interfaces

42 interfaces between chains.

  • L–O · 546 Ų buried · 10 hydrogen bonds · protein-protein
  • F–J · 544 Ų buried · 12 hydrogen bonds · protein-protein
  • K–O · 542 Ų buried · 12 hydrogen bonds · protein-protein
  • B–E · 542 Ų buried · 11 hydrogen bonds · protein-protein
  • R–S · 532 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 6LUK · Crystal structure of the SAMD1 SAM domain in another crystal form · the same entry in another collection · chain T against T, TM-score 1.00

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