Research workbench
E. COLI aminopeptidase P in complex with substrate
Analyse E. COLI aminopeptidase P in complex with substrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BHA
- Type
- protein
- Length
- 443 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xaa-pro aminopeptidase; Valine-proline-leucine
- EC
- 3.4.11.9
- UniProt
- P15034
- Ligands
- MG
- Pockets
- 4 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xaa-pro aminopeptidase (EC 3.4.11.9) | protein | 440 | 40% helix, 18% strand | P15034 |
| B | Valine-proline-leucine | protein | 3 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.46 | 0.77 | 19 | empty |
| 2 | 74 | 0.31 | 0.74 | 16 | empty |
| 3 | 70 | 0.31 | 0.74 | 18 | empty |
| 4 | 61 | 0.31 | 0.75 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 359 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
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 P15034
- Elsewhere: RCSB PDB 2BHA · PDBe 2BHA · UniProt P15034
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.