MolNFT v1 · #127504 · protein
Convergent evolution involving dimeric and trimeric dutpases in signalling.
5MYI · Dutpase from di S. aureus phage: “Convergent evolution involving dimeric and trimeric dutpases in signalling.”. X-ray diffraction, 3 ligands (CA, MG, CL). MolNFT v1 #127504 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5MYI
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dutpase from di S. aureus phage
- EC
- 3.6.1.23
- Ligands
- CA, MG, CL
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Dutpase from di S. aureus phage (EC 3.6.1.23) | protein | 165 | 70% helix, 0% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains D
- MG · Magnesium ion · metal · chains D
- CL · Chloride ion · ion · chains D
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5MYI · Convergent evolution involving dimeric and trimeric dUTPases in signalling. · the same entry in another collection · chain D against D, 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
- Elsewhere: RCSB PDB 5MYI · PDBe 5MYI
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