MolNFT v1 · #153757 · protein
Crystal structures of phage nrs-1 N300-dntps-MG2+ complex provide molecular mechanisms for substrate specificity
6JON: “Crystal structures of phage nrs-1 N300-dntps-MG2+ complex provide molecular mechanisms for substrate…”. X-ray diffraction, 2 ligands (DTP, MG). MolNFT v1 #153757 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6JON
- Type
- protein
- Length
- 280 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- M5AAG8
- Ligands
- DTP, MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 280 | — | M5AAG8 |
Ligands and binding sites
- DTP · 2'-deoxyadenosine 5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6JON · Crystal structures of phage NrS-1 N300-dNTPs-Mg2+ complex provide molecular mechanisms… · the same entry in another collection · chain A 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 M5AAG8
- Elsewhere: RCSB PDB 6JON · PDBe 6JON · UniProt M5AAG8
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