Research workbench
Structural and functional analysis of the E. COLI ftsz interacting protein, zapc, reveals insight into molecular properties of a novel Z ring stabilizing protein
Analyse Structural and functional analysis of the E. COLI ftsz interacting protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5E1L
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein zapc
- UniProt
- W8SPQ2
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein zapc | protein | 173 | 24% helix, 34% strand | W8SPQ2 |
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 | 120 | 0.43 | 0.76 | 20 | empty |
| 2 | 50 | 0.36 | 0.80 | 12 | empty |
Compared structures
- 5E1L · Structural and functional analysis of the E. coli FtsZ interacting protein, ZapC, reveals… · 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 W8SPQ2
- Elsewhere: RCSB PDB 5E1L · PDBe 5E1L · UniProt W8SPQ2
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