Research workbench
ADAMTS13-CUB12
Analyse ADAMTS13-CUB12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7B01
- Type
- protein
- Length
- 588 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltodextrin-binding PROTEIN,MALTODEXTRIN-binding protein, maltodextrin-binding…
- EC
- 3.4.24.87
- UniProt
- A0A376KDN7, Q76LX8
- Ligands
- NAG, GLC
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltodextrin-binding PROTEIN,MALTODEXTRIN-binding protein, maltodextrin-binding PROTEIN,ADAMTS13 CUB12,A disintegrin and metalloproteinase with thrombospondin motifs 13,A disintegrin and metalloproteinase with thrombospondin motifs 13,A disintegrin and metalloproteinase with thrombospondin motifs 13 (EC 3.4.24.87) | protein | 588 | 28% helix, 27% strand | A0A376KDN7, Q76LX8 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.71 | 0.85 | 25 | GLC |
| 2 | 526 | 0.68 | 0.79 | 59 | empty |
| 3 | 108 | 0.40 | 0.76 | 15 | empty |
| 4 | 96 | 0.37 | 0.75 | 19 | empty |
| 5 | 56 | 0.35 | 0.78 | 18 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 A0A376KDN7
- Every structure of UniProt Q76LX8
- Elsewhere: RCSB PDB 7B01 · PDBe 7B01 · UniProt A0A376KDN7 · UniProt Q76LX8
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