Research workbench
GLU383ALA escherichia COLI aminopeptidase P
Analyse GLU383ALA escherichia COLI aminopeptidase P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BWY
- Type
- protein
- Length
- 440 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminopeptidase P
- EC
- 3.4.11.9
- UniProt
- P15034
- Ligands
- MN, MG, SO4
- Pockets
- 5 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminopeptidase P (EC 3.4.11.9) | protein | 440 | 40% helix, 18% strand | P15034 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- FLC · Citrate anion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.47 | 0.80 | 21 | MN, SO4 |
| 2 | 131 | 0.44 | 0.76 | 19 | empty |
| 3 | 62 | 0.32 | 0.76 | 17 | empty |
| 4 | 65 | 0.31 | 0.75 | 11 | empty |
| 5 | 62 | 0.28 | 0.74 | 16 | empty |
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 2BWY · PDBe 2BWY · UniProt P15034
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