MolNFT v1 · #57036 · protein
Crystal structure of peptidoglycan hydrolase from sphingomonas sp. A1
2ZYC · Peptidoglycan hydrolase flgj: “Crystal structure of peptidoglycan hydrolase from sphingomonas sp. A1”. X-ray diffraction, 1 ligand (PO4), 1 pocket (best druggability 0.25). MolNFT v1 #57036 on GenesisL1: 3D structure, binding sites…
- PDB
- 2ZYC
- Type
- protein
- Length
- 156 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidoglycan hydrolase flgj
- EC
- 3.2.1.-
- UniProt
- B7XH69
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.25
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidoglycan hydrolase flgj (EC 3.2.1.-) | protein | 156 | 49% helix, 11% strand | B7XH69 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 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 | 53 | 0.25 | 0.72 | 13 | empty |
Compared structures
- 2ZYC · Crystal structure of peptidoglycan hydrolase 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 2ZYC · PDBe 2ZYC · UniProt B7XH69
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