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X-ray structure of the fefe-hydrogenase maturase hyde from T. maritima in complex with S-adenosyl-L-methionine

Analyse X-ray structure of the fefe-hydrogenase maturase hyde from T. maritima in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3IIZ
Type
protein
Length
346 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Biotin synthetase, putative
UniProt
Q9X0Z6
Ligands
CPS, SF4, SAM, FES, H2S, CL, CO3
Pockets
2 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABiotin synthetase, putativeprotein34642% helix, 13% strandQ9X0Z6

Ligands and binding sites

  • CPS · 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate · ligand · 5 copies · chains A
  • SF4 · Iron/sulfur cluster · ligand · chains A
  • SAM · S-adenosylmethionine · ligand · chains A
  • FES · Fe2/s2 (inorganic) cluster · ligand · chains A
  • H2S · Hydrosulfuric acid · ion · 2 copies · chains A
  • CL · Chloride ion · ion · 2 copies · chains A
  • CO3 · Carbonate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14470.880.9557SF4, SAM, CL
2530.320.7715empty

Modifications

Observed in the structure: 2 modified (nonstandard, oxidation).

Compared structures

  • 3IIZ · X-ray structure of the FeFe-hydrogenase maturase HydE from T. maritima in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9X0Z6 · AlphaFold monomer V2.0 prediction for [fefe] hydrogenase maturase subunit hyde (Q9X0Z6) · a predicted model of the same protein · chain A against A, TM-score 1.00

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