Research workbench
Crystal structure of the adenosylmethionine decarboxylase (AQ_254) from aquifex aeolicus VF5
Analyse Crystal structure of the adenosylmethionine decarboxylase (AQ_254) from aquifex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2III
- Type
- protein
- Length
- 120 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-adenosylmethionine decarboxylase proenzyme
- EC
- 4.1.1.50
- UniProt
- O66615
- Ligands
- MG, CA
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosylmethionine decarboxylase proenzyme (EC 4.1.1.50) | protein | 120 | 29% helix, 46% strand | O66615 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (engineered).
Compared structures
- 2III · Crystal structure of the adenosylmethionine decarboxylase (aq_254) from aquifex aeolicus… · the same entry in another collection · chain A against A, TM-score 1.00
- O66615 · AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme… · a predicted model of the same protein · chain A 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 O66615
- Elsewhere: RCSB PDB 2III · PDBe 2III · UniProt O66615
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