Research workbench
Crystal structures of cyanuric acid hydrolase from moorella thermoacetica
Analyse Crystal structures of cyanuric acid hydrolase from moorella thermoacetica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DHJ
- Type
- protein
- Length
- 2,897 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyanuric acid amidohydrolase
- EC
- 3.5.2.15
- UniProt
- Q2RGM7
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 6 distinct chains · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyanuric acid amidohydrolase (EC 3.5.2.15) | protein | 365 | 35% helix, 28% strand | Q2RGM7 |
| B, H | Cyanuric acid amidohydrolase (EC 3.5.2.15) | protein | 363 | 35% helix, 26% strand | Q2RGM7 |
| C | Cyanuric acid amidohydrolase (EC 3.5.2.15) | protein | 362 | 35% helix, 26% strand | Q2RGM7 |
| D, E | Cyanuric acid amidohydrolase (EC 3.5.2.15) | protein | 364 | 35% helix, 26% strand | Q2RGM7 |
| F | Cyanuric acid amidohydrolase (EC 3.5.2.15) | protein | 357 | 36% helix, 26% strand | Q2RGM7 |
| G | Cyanuric acid amidohydrolase (EC 3.5.2.15) | protein | 359 | 36% helix, 26% strand | Q2RGM7 |
Ligands and binding sites
- CIT · Citric acid · additive · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 882 | 0.79 | 0.82 | 118 | CIT |
| 2 | 1072 | 0.78 | 0.80 | 125 | CIT |
| 3 | 1089 | 0.76 | 0.79 | 118 | CIT |
| 4 | 637 | 0.74 | 0.81 | 96 | CIT |
| 5 | 1031 | 0.74 | 0.77 | 99 | empty |
Interfaces
15 interfaces between chains.
- B–D · 1516 Ų buried · 19 hydrogen bonds · protein-protein
- A–F · 1512 Ų buried · 20 hydrogen bonds · protein-protein
- E–H · 1508 Ų buried · 20 hydrogen bonds · protein-protein
- C–G · 1483 Ų buried · 16 hydrogen bonds · protein-protein
- F–H · 678 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 covalent, 4 disulfide (additive adduct, disulfide).
Compared structures
- 6DHJ · Crystal structures of cyanuric acid hydrolase from Moorella thermoacetica · the same entry in another collection · chain F against F, TM-score 1.00
- Q2RGM7 · AlphaFold monomer V2.0 prediction for cyanuric acid amidohydrolase (Q2RGM7) · a predicted model of the same protein · chain E against A, TM-score 0.97
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 Q2RGM7
- Elsewhere: RCSB PDB 6DHJ · PDBe 6DHJ · UniProt Q2RGM7
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