Research workbench
Crystal structure of human AMDHD2 in complex with zn
Analyse Crystal structure of human AMDHD2 in complex with zn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NUU
- Type
- protein
- Length
- 797 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetylglucosamine-6-phosphate deacetylase
- EC
- 3.5.1.25
- UniProt
- Q9Y303
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) | protein | 398 | 27% helix, 28% strand | Q9Y303 |
| B | N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) | protein | 399 | 27% helix, 27% strand | Q9Y303 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.57 | 0.83 | 33 | GOL |
| 2 | 155 | 0.57 | 0.82 | 33 | ZN, GOL |
| 3 | 55 | 0.33 | 0.77 | 16 | empty |
| 4 | 76 | 0.28 | 0.73 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1094 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 7NUU · Crystal structure of human AMDHD2 in complex with Zn · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y303 · AlphaFold monomer V2.0 prediction for N-acetylglucosamine-6-phosphate deacetylase (Q9Y303) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9Y303
- Elsewhere: RCSB PDB 7NUU · PDBe 7NUU · UniProt Q9Y303
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.