Research workbench
Ftse structure of streptococcus pneumoniae in complex with amppnp at 2.4 a resolution
Analyse Ftse structure of streptococcus pneumoniae in complex with amppnp at 2.4 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Z67
- Type
- protein
- Length
- 681 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division ATP-binding protein ftse
- UniProt
- A0A064BZ20
- Ligands
- ANP, ADP
- Pockets
- 6 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, B | Cell division ATP-binding protein ftse | protein | 229 | 37% helix, 25% strand | A0A064BZ20 |
| E | Cell division ATP-binding protein ftse | protein | 223 | 36% helix, 26% strand | A0A064BZ20 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains B, E
- ADP · Adenosine-5'-diphosphate · ligand · chains C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 538 | 0.65 | 0.76 | 44 | ADP |
| 2 | 240 | 0.60 | 0.81 | 36 | ANP |
| 3 | 297 | 0.58 | 0.77 | 34 | empty |
| 4 | 195 | 0.54 | 0.78 | 24 | empty |
| 5 | 197 | 0.51 | 0.77 | 27 | empty |
Interfaces
3 interfaces between chains.
- B–E · 466 Ų buried · 13 hydrogen bonds · protein-protein
- C–B · 290 Ų buried · 4 hydrogen bonds · protein-protein
- C–E · 274 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6Z67 · FtsE structure of Streptococcus pneumoniae in complex with AMPPNP at 2.4 A resolution · the same entry in another collection · chain C against C, 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 A0A064BZ20
- Elsewhere: RCSB PDB 6Z67 · PDBe 6Z67 · UniProt A0A064BZ20
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