Research workbench
Crystal structure of an enterococcus faecium peptidoglycan binding protein at 2.4 a resolution
Analyse Crystal structure of an enterococcus faecium peptidoglycan binding protein at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZAT
- Type
- protein
- Length
- 248 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L,D-transpeptidase
- UniProt
- Q3Y185
- Ligands
- ZN, SO4
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L,D-transpeptidase | protein | 248 | 25% helix, 34% strand | Q3Y185 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.36 | 0.78 | 20 | ZN |
| 2 | 89 | 0.36 | 0.75 | 20 | empty |
Compared structures
- 1ZAT · Crystal Structure of an Enterococcus faecium peptidoglycan binding protein at 2.4 A… · 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 Q3Y185
- Elsewhere: RCSB PDB 1ZAT · PDBe 1ZAT · UniProt Q3Y185
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