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Crystal structure of the hypc-hypd complex

Analyse Crystal structure of the hypc-hypd complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3VYR
Type
protein
Length
443 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hydrogenase EXPRESSION/FORMATION protein hypc; Hydrogenase EXPRESSION/FORMATION protein…
UniProt
Q5JII0, Q5JII1
Ligands
SF4
Pockets
4 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHydrogenase EXPRESSION/FORMATION protein hypcprotein7226% helix, 40% strandQ5JII0
BHydrogenase EXPRESSION/FORMATION protein hypdprotein37145% helix, 18% strandQ5JII1

Ligands and binding sites

  • SF4 · Iron/sulfur cluster · ligand · chains B
  • CIT · Citric acid · additive · 7 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15380.720.8062CIT
21980.480.7538empty
31720.460.7520empty
41130.390.7523empty

Interfaces

1 interface between chains.

  • A–B · 1145 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 3VYR · Crystal structure of the HypC-HypD complex · the same entry in another collection · chain A against A, TM-score 1.00

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