MolNFT v1 · #121521 · protein
Structure-function analysis of functionally diverse members of the cyclic amide hydrolase family of toblerone fold enzymes
5HY2 · Ring-opening amidohydrolase: “Structure-function analysis of functionally diverse members of the cyclic amide hydrolase family of toblerone…”. X-ray diffraction, 5 pockets (best druggability 0.65). MolNFT v1 #121521 on GenesisL1: 3D…
- PDB
- 5HY2
- Type
- protein
- Length
- 667 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ring-opening amidohydrolase
- EC
- 3.5.2.15
- UniProt
- E3JD18
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ring-opening amidohydrolase (EC 3.5.2.15) | protein | 337 | 29% helix, 28% strand | E3JD18 |
| B | Ring-opening amidohydrolase (EC 3.5.2.15) | protein | 330 | 29% helix, 29% strand | E3JD18 |
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 221 | 0.65 | 0.84 | 34 | empty |
| 2 | 353 | 0.65 | 0.80 | 51 | empty |
| 3 | 403 | 0.64 | 0.79 | 51 | empty |
| 4 | 223 | 0.61 | 0.81 | 37 | empty |
| 5 | 177 | 0.57 | 0.81 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1480 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5HY2 · Structure-function analysis of functionally diverse members of the cyclic amide hydrolase… · the same entry in another collection · chain A against A, TM-score 1.00
- E3JD18 · AlphaFold monomer V2.0 prediction for cyclic amide hydrolase (E3JD18) · a predicted model of the same protein · chain B 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 E3JD18
- Elsewhere: RCSB PDB 5HY2 · PDBe 5HY2 · UniProt E3JD18
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