Research workbench
Crystal structure of the catalytic domain of human adam 33
Analyse Crystal structure of the catalytic domain of human adam 33 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R55
- Type
- protein
- Length
- 203 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adam 33
- EC
- 3.4.24.-
- UniProt
- Q9BZ11
- Ligands
- 097, MAN, NAG, ZN, CA, CL
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adam 33 (EC 3.4.24.-) | protein | 203 | 41% helix, 17% strand | Q9BZ11 |
Ligands and binding sites
- 097 · (2S,3R)-N~4~-[(1S)-2,2-dimethyl-1-(methylcarbamoyl)propyl]-N~1~,2-dihydroxy-3-(2-methylpropyl)butanediamide · ligand · chains A
- MAN · alpha-D-mannopyranose · sugar · 3 copies
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- ZN · Zinc ion · metal · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.40 | 0.77 | 28 | ZN, 097 |
Modifications
Observed in the structure: 3 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 1R55 · Crystal structure of the catalytic domain of human ADAM 33 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BZ11 · AlphaFold monomer V2.0 prediction for disintegrin and metalloproteinase domain-containing… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9BZ11
- Elsewhere: RCSB PDB 1R55 · PDBe 1R55 · UniProt Q9BZ11
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