MolNFT v1 · #162162 · protein
Getah virus macro domain in complex with adpr covalently bond to CYS34
6R0R: “Getah virus macro domain in complex with adpr covalently bond to CYS34”. X-ray diffraction, 1 ligand (JNT). MolNFT v1 #162162 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6R0R
- Type
- protein
- Length
- 162 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A143SL92
- Ligands
- JNT
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 162 | — | A0A143SL92 |
Ligands and binding sites
- JNT · [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{S})-2,3,4,5-tetrakis(oxidanyl)pentyl] hydrogen phosphate · ligand · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6R0R · Getah virus macro domain in complex with ADPr covalently bond to Cys34 · 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 A0A143SL92
- Elsewhere: RCSB PDB 6R0R · PDBe 6R0R · UniProt A0A143SL92
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