MolNFT v1 · #171469 · protein
Ftse structure from streptococus pneumoniae in complex with ADP at 1.57 a resolution (spacegroup P 21)
6Z63 · Cell division ATP-binding protein ftse: “Ftse structure from streptococus pneumoniae in complex with ADP at 1.57 a resolution (spacegroup P 21)”. X-ray diffraction, 1 ligand (ADP), 6 pockets (best druggability 0.71). MolNFT v1…
- PDB
- 6Z63
- Type
- protein
- Length
- 686 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
- ADP
- Pockets
- 6 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division ATP-binding protein ftse | protein | 228 | 34% helix, 25% strand | A0A064BZ20 |
| B, C | Cell division ATP-binding protein ftse | protein | 229 | 36% helix, 25% strand | A0A064BZ20 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 651 | 0.71 | 0.79 | 56 | ADP |
| 2 | 297 | 0.62 | 0.80 | 48 | ADP |
| 3 | 358 | 0.59 | 0.77 | 39 | empty |
| 4 | 222 | 0.54 | 0.77 | 21 | empty |
| 5 | 199 | 0.53 | 0.78 | 24 | empty |
Interfaces
3 interfaces between chains.
- A–B · 474 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 262 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 260 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6Z63 · FtsE structure from Streptococus pneumoniae in complex with ADP at 1.57 A resolution… · 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 A0A064BZ20
- Elsewhere: RCSB PDB 6Z63 · PDBe 6Z63 · UniProt A0A064BZ20
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