MolNFT v1 · #82758 · protein
Crystal structure of peptidoglycan hydrolase mutant from sphingomonas sp. A1
3VWO · Peptidoglycan hydrolase flgj: “Crystal structure of peptidoglycan hydrolase mutant from sphingomonas sp. A1”. X-ray diffraction, 1 pocket (best druggability 0.56). MolNFT v1 #82758 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3VWO
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidoglycan hydrolase flgj
- UniProt
- B7XH69
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidoglycan hydrolase flgj | protein | 155 | 49% helix, 15% strand | B7XH69 |
Ligands and binding sites
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 280 | 0.56 | 0.76 | 27 | EPE |
Compared structures
- 3VWO · Crystal structure of peptidoglycan hydrolase mutant from Sphingomonas sp. A1 · 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 B7XH69
- Elsewhere: RCSB PDB 3VWO · PDBe 3VWO · UniProt B7XH69
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