MolNFT v1 · #142290 · protein
Crystal structure of peg-1500 crystallized peptidyl-tRNA hydrolase from acinetobacter baumannii at 1.5 a resolution
5ZZV: “Crystal structure of peg-1500 crystallized peptidyl-tRNA hydrolase from acinetobacter baumannii at 1.5 a…”. X-ray diffraction, 1 pocket (best druggability 0.36). MolNFT v1 #142290 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5ZZV
- Type
- protein
- Length
- 193 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-tRNA hydrolase
- EC
- 3.1.1.29
- UniProt
- D0C9L6
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase (EC 3.1.1.29) | protein | 193 | 41% helix, 22% strand | D0C9L6 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.36 | 0.78 | 21 | empty |
Compared structures
- 5ZZV · Crystal structure of PEG-1500 crystallized Peptidyl-tRNA Hydrolase from Acinetobacter… · 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 D0C9L6
- Elsewhere: RCSB PDB 5ZZV · PDBe 5ZZV · UniProt D0C9L6
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