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Crystal structure of A102D mutant of HSP14.1 from sulfolobus solfatataricus P2

Analyse Crystal structure of A102D mutant of HSP14.1 from sulfolobus solfatataricus P2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4YLB
Type
protein
Length
491 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heat shock protein HSP20
UniProt
D0KNS6
Ligands
CL
Pockets
5 · best druggability 0.63

Structure

x-ray diffraction · 4 distinct chains · 15% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHeat shock protein HSP20protein12819% helix, 41% strandD0KNS6
BHeat shock protein HSP20protein11714% helix, 43% strandD0KNS6
CHeat shock protein HSP20protein12713% helix, 40% strandD0KNS6
DHeat shock protein HSP20protein11915% helix, 39% strandD0KNS6

Ligands and binding sites

  • CL · Chloride ion · ion · 3 copies · chains A, B, D

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15220.630.7658empty
2760.550.8627empty
3650.300.7417empty
4740.280.7219empty
5540.260.7419empty

Interfaces

5 interfaces between chains.

  • C–D · 1974 Ų buried · 40 hydrogen bonds · protein-protein
  • A–B · 1965 Ų buried · 42 hydrogen bonds · protein-protein
  • A–C · 942 Ų buried · 14 hydrogen bonds · protein-protein
  • A–D · 370 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 367 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 4YLB · Crystal Structure of A102D mutant of hsp14.1 from Sulfolobus solfatataricus P2 · the same entry in another collection · chain A against A, TM-score 1.00

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