MolNFT v1 · #66512 · protein
Crystal structure of human collagen xviii trimerization domain (tetragonal crystal form)
3HSH · Collagen alpha-1(XVIII) chain: “Crystal structure of human collagen xviii trimerization domain (tetragonal crystal form)”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #66512 on GenesisL1: 3D structure, binding sites and pockets in…
- 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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F | Collagen alpha-1(XVIII) chain | protein | 56 | 18% helix, 46% strand | P39060 |
| E | Collagen alpha-1(XVIII) chain | protein | 55 | 18% helix, 42% strand | P39060 |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P39060
- Elsewhere: RCSB PDB 3HSH · PDBe 3HSH · UniProt P39060
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