MolNFT v1 · #126452 · protein
Macrodomain of thermus aquaticus darg in complex with ADP-ribose
5M3E · Appr-1-P processing domain protein: “Macrodomain of thermus aquaticus darg in complex with ADP-ribose”. X-ray diffraction, 2 ligands (APR, CL), 1 pocket (best druggability 0.59). MolNFT v1 #126452 on GenesisL1: 3D structure, binding…
- PDB
- 5M3E
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Appr-1-P processing domain protein
- UniProt
- B7A854
- Ligands
- APR, CL
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Appr-1-P processing domain protein | protein | 152 | 36% helix, 20% strand | B7A854 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.59 | 0.82 | 31 | APR, CL |
Compared structures
- 5M3E · Macrodomain of Thermus aquaticus DarG in complex with ADP-ribose · 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 B7A854
- Elsewhere: RCSB PDB 5M3E · PDBe 5M3E · UniProt B7A854
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