MolNFT v1 · #52756 · protein
Structural basis of N-end rule substrate recognition in escherichia COLI by the clpap adaptor protein clps - TRP peptide structure
2WA9 · ATP-dependent clp protease adapter protein clps: “Structural basis of N-end rule substrate recognition in escherichia COLI by the clpap adaptor protein clps…”. X-ray diffraction, 5 pockets (best druggability 0.69). MolNFT v1 #52756…
- PDB
- 2WA9
- Type
- protein
- Length
- 616 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease adapter protein clps; TRP peptide
- UniProt
- P0A8Q6
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 5 distinct chains · 49% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease adapter protein clps | protein | 83 | 51% helix, 27% strand | P0A8Q6 |
| B, C, D, E, F | ATP-dependent clp protease adapter protein clps | protein | 86 | 50% helix, 26% strand | P0A8Q6 |
| G | ATP-dependent clp protease adapter protein clps | protein | 83 | 51% helix, 23% strand | P0A8Q6 |
| H, I, J, K, L, M | TRP peptide | protein | 3 | 0% helix, 0% strand | — |
| N | TRP peptide | protein | 2 | 0% helix, 0% strand | — |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 700 | 0.69 | 0.76 | 72 | empty |
| 2 | 266 | 0.57 | 0.77 | 28 | empty |
| 3 | 349 | 0.56 | 0.75 | 35 | empty |
| 4 | 96 | 0.42 | 0.77 | 20 | empty |
| 5 | 62 | 0.30 | 0.75 | 14 | empty |
Interfaces
25 interfaces between chains.
- B–C · 802 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 731 Ų buried · 6 hydrogen bonds · protein-protein
- D–F · 424 Ų buried · 4 hydrogen bonds · protein-protein
- C–G · 367 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 361 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2WA9 · Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP… · the same entry in another collection · chain M against M, 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 P0A8Q6
- Elsewhere: RCSB PDB 2WA9 · PDBe 2WA9 · UniProt P0A8Q6
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