Research workbench
Crystal structure of H.PYLORI clpp S99A in complex with the peptide aaaa
Analyse Crystal structure of H.PYLORI clpp S99A in complex with the peptide aaaa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZL4
- Type
- protein
- Length
- 2,478 residues
- Chains
- 28
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit; Peptide substrate aaaa
- EC
- 3.4.21.92
- UniProt
- P56156
- Pockets
- 20 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 173 | 49% helix, 26% strand | P56156 |
| O, P, Q, R, S, T, U, V, W, X, Y, Z, 1, 2 | Peptide substrate aaaa | protein | 4 | 0% helix, 25% strand | — |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 496 | 0.63 | 0.76 | 67 | empty |
| 2 | 474 | 0.62 | 0.75 | 65 | empty |
| 3 | 465 | 0.62 | 0.76 | 59 | empty |
| 4 | 428 | 0.61 | 0.76 | 71 | empty |
| 5 | 452 | 0.61 | 0.76 | 62 | empty |
Interfaces
63 interfaces between chains.
- A–G · 1182 Ų buried · 10 hydrogen bonds · protein-protein
- H–I · 1182 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 1175 Ų buried · 8 hydrogen bonds · protein-protein
- E–F · 1174 Ų buried · 9 hydrogen bonds · protein-protein
- F–G · 1173 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2ZL4 · Crystal structure of H.pylori ClpP S99A in complex with the peptide AAAA · the same entry in another collection · chain T against T, 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 P56156
- Elsewhere: RCSB PDB 2ZL4 · PDBe 2ZL4 · UniProt P56156
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