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Structure of fully reduced hydrogenase (hyd-1)

Analyse Structure of fully reduced hydrogenase (hyd-1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6FPW
Type
protein
Length
1,690 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P69739, P0ACD8
Ligands
SF4, F3S, SF3, EJ2, MG, CL, SO4

Structure

x-ray diffraction · 2 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
S, T—protein264—P69739
L, M—protein581—P0ACD8

Ligands and binding sites

  • SF4 · Iron/sulfur cluster · ligand · 2 copies · chains S, T
  • F3S · FE3-S4 cluster · ligand · 2 copies · chains S, L, T, M
  • SF3 · FE4-S3 cluster · ligand · 2 copies · chains S, L, T, M
  • EJ2 · Ni-Fe reduced active center · ligand · 2 copies · chains L, M
  • MG · Magnesium ion · metal · 2 copies · chains L, M
  • CL · Chloride ion · ion · 6 copies · chains S, T
  • SO4 · Sulfate ion · ion · chains S, L
  • LMT · Dodecyl-beta-D-maltoside · additive · 2 copies · chains S, T

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

Compared structures

  • 6FPW · Structure of fully reduced Hydrogenase (Hyd-1) · the same entry in another collection · chain S against S, TM-score 1.00
  • P0ACD8 · AlphaFold monomer V2.0 prediction for hydrogenase-1 large chain (P0ACD8) · a predicted model of the same protein · chain L against A, TM-score 1.00
  • P69739 · AlphaFold monomer V2.0 prediction for hydrogenase-1 small chain (P69739) · a predicted model of the same protein · chain S against A, TM-score 1.00

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