MolNFT v2 · #118394 · protein
Crystal structure of elongation domain of Phomopsis amygdali fusicoccadiene synthase complexed with cobalt ions and pamidronate
5ERO: “Crystal structure of elongation domain of Phomopsis amygdali fusicoccadiene synthase complexed with cobalt…”. X-ray diffraction at 2.55, 2 ligands (210, CO). MolNFT v2 #118394 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5ERO
- Type
- protein
- Length
- 900 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.55
- Source
- Phomopsis amygdali
- UniProt
- A2PZA5
- Ligands
- 210, CO
Structure
x-ray diffraction · resolution 2.55 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 301 | — | A2PZA5 |
| B | — | protein | 300 | — | A2PZA5 |
| C | — | protein | 299 | — | A2PZA5 |
Ligands and binding sites
- 210 · Pamidronate · ligand · 3 copies · chains A, B, C
- CO · Cobalt (II) ion · metal · 12 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5ERO · Crystal structure of elongation domain of phomopsis amygdali fusicoccadiene synthase… · the same entry in another collection · chain A against A, TM-score 1.00
- A2PZA5 · AlphaFold monomer V2.0 prediction for fusicoccadiene synthase (A2PZA5) · a predicted model of the same protein · chain C 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 A2PZA5
- Elsewhere: RCSB PDB 5ERO · PDBe 5ERO · UniProt A2PZA5
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