MolNFT v1 · #135269 · protein
Crystal structure of staphylococcus epidermidis aap G511-spacer-G513 (consensus G5-spacer-consensus G5)
5TU7 · Accumulation-associated protein aap G511-spacer-G513…: “Crystal structure of staphylococcus epidermidis aap G511-spacer-G513 (consensus G5-spacer-consensus G5)”. X-ray diffraction, 3 pockets (best druggability 0.46). MolNFT v1…
- PDB
- 5TU7
- Type
- protein
- Length
- 259 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Accumulation-associated protein aap G511-spacer-G513 (consensus G5-spacer-consensus G5)
- UniProt
- Q5HKE8
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Accumulation-associated protein aap G511-spacer-G513 (consensus G5-spacer-consensus G5) | protein | 132 | 0% helix, 49% strand | Q5HKE8 |
| B | Accumulation-associated protein aap G511-spacer-G513 (consensus G5-spacer-consensus G5) | protein | 127 | 0% helix, 55% strand | Q5HKE8 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.46 | 0.78 | 20 | empty |
| 2 | 72 | 0.31 | 0.74 | 15 | empty |
| 3 | 50 | 0.23 | 0.72 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 714 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 5TU7 · Crystal structure of Staphylococcus epidermidis Aap G511-spacer-G513 (consensus… · 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 Q5HKE8
- Elsewhere: RCSB PDB 5TU7 · PDBe 5TU7 · UniProt Q5HKE8
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