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Crystal structure of human collagen xviii trimerization domain (tetragonal crystal form)

Analyse Crystal structure of human collagen xviii trimerization domain (tetragonal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3HSH
Type
protein
Length
335 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Collagen alpha-1(XVIII) chain
UniProt
P39060
Ligands
SO4

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, FCollagen alpha-1(XVIII) chainprotein5618% helix, 46% strandP39060
ECollagen alpha-1(XVIII) chainprotein5518% helix, 42% strandP39060

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 13 copies · chains A, B, C, D, F, E
  • GOL · Glycerol · additive · 9 copies · chains A, B, C, D

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

Interfaces

10 interfaces between chains.

  • E–F · 1059 Ų buried · 10 hydrogen bonds · protein-protein
  • D–F · 1057 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 1047 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 1043 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 1034 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 3HSH · Crystal structure of human collagen XVIII trimerization domain (Tetragonal crystal form) · the same entry in another collection · chain F against F, TM-score 1.00
  • P39060 · AlphaFold monomer V2.0 prediction for collagen alpha-1(XVIII) chain (P39060) · a predicted model of the same protein · chain E against A, TM-score 0.84

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