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Crystal structure of hypc from thermococcus kodakaraensis KOD1

Analyse Crystal structure of hypc from thermococcus kodakaraensis KOD1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Z1C
Type
protein
Length
216 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hydrogenase EXPRESSION/FORMATION protein hypc
UniProt
Q5JII0
Pockets
1 · best druggability 0.68

Structure

x-ray diffraction · 3 distinct chains · 25% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHydrogenase EXPRESSION/FORMATION protein hypcprotein7124% helix, 42% strandQ5JII0
BHydrogenase EXPRESSION/FORMATION protein hypcprotein7426% helix, 41% strandQ5JII0
CHydrogenase EXPRESSION/FORMATION protein hypcprotein7125% helix, 35% strandQ5JII0

Ligands and binding sites

  • GOL · Glycerol · additive · chains A, C
  • PG4 · Tetraethylene glycol · additive · chains B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15820.680.7758GOL, PG4

Interfaces

3 interfaces between chains.

  • B–C · 720 Ų buried · 8 hydrogen bonds · protein-protein
  • A–B · 348 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 75 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 2Z1C · Crystal structure of HypC from Thermococcus kodakaraensis KOD1 · the same entry in another collection · chain A against A, TM-score 1.00

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