Research workbench
An unexpected vestigial protein complex reveals the evolutionary origins of an S-triazine catabolic enzyme.
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
- 6C62
- Type
- protein
- Length
- 1,046 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q936X3
- Ligands
- MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 457 | — | Q936X3 |
| C, D | — | protein | 66 | — | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6C62 · 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 6C62 · PDBe 6C62 · UniProt Q936X3
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