Research workbench
An unexpected vestigial protein complex reveals the evolutionary origins of an S-triazine catabolic enzyme. inhibitor bound complex.
Analyse An unexpected vestigial protein complex reveals the evolutionary origins of an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C6G
- Type
- protein
- Length
- 1,046 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biuret hydrolase; Atzg
- EC
- 3.5.1.84
- UniProt
- Q936X3
- Ligands
- CA
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Biuret hydrolase (EC 3.5.1.84) | protein | 457 | 41% helix, 16% strand | Q936X3 |
| C, D | Atzg | protein | 66 | 56% helix, 0% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 882 | 0.77 | 0.80 | 91 | empty |
| 2 | 209 | 0.63 | 0.83 | 40 | empty |
| 3 | 158 | 0.52 | 0.79 | 27 | empty |
| 4 | 159 | 0.50 | 0.78 | 23 | empty |
| 5 | 168 | 0.48 | 0.77 | 22 | empty |
Interfaces
4 interfaces between chains.
- B–C · 1591 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 1591 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 277 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 242 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 6C6G · An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine… · the same entry in another collection · chain A against A, TM-score 1.00
- Q936X3 · AlphaFold monomer V2.0 prediction for 1-carboxybiuret hydrolase subunit atze (Q936X3) · a predicted model of the same protein · chain B against A, TM-score 1.00
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 Q936X3
- Elsewhere: RCSB PDB 6C6G · PDBe 6C6G · UniProt Q936X3
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