Research workbench
Crystal structure of the exosite-containing fragment of human ADAMTS13 (form-1)
Analyse Crystal structure of the exosite-containing fragment of human ADAMTS13 (form-1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GHM
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- A disintegrin and metalloproteinase with thrombospondin motifs 13
- EC
- 3.4.24.-
- UniProt
- Q76LX8
- Ligands
- NAG, FUC, BGC
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | A disintegrin and metalloproteinase with thrombospondin motifs 13 (EC 3.4.24.-) | protein | 369 | 9% helix, 33% strand | Q76LX8 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- FUC · alpha-L-fucopyranose · sugar · chains A
- BGC · beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 419 | 0.66 | 0.79 | 53 | BGC |
Modifications
Observed in the structure: 12 disulfide, 3 glycan (disulfide, N-glycosylation, O-glycosylation).
Compared structures
- 3GHM · Crystal structure of the exosite-containing fragment of human ADAMTS13 (form-1) · the same entry in another collection · chain A against A, TM-score 1.00
- Q76LX8 · AlphaFold monomer V2.0 prediction for a disintegrin and metalloproteinase with… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q76LX8
- Elsewhere: RCSB PDB 3GHM · PDBe 3GHM · UniProt Q76LX8
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