MolNFT v1 · #14246 · protein
Aminopeptidase P from escherichia COLI
1M35: “Aminopeptidase P from escherichia COLI”. X-ray diffraction, 1 ligand (MN), 20 pockets (best druggability 0.86). MolNFT v1 #14246 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1M35
- Type
- protein
- Length
- 2,640 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminopeptidase P
- EC
- 3.4.11.9
- UniProt
- P15034
- Ligands
- MN
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Aminopeptidase P (EC 3.4.11.9) | protein | 440 | 41% helix, 19% strand | P15034 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 12 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 923 | 0.86 | 0.88 | 96 | MN |
| 2 | 306 | 0.83 | 0.94 | 43 | empty |
| 3 | 1190 | 0.82 | 0.83 | 107 | MN |
| 4 | 1156 | 0.81 | 0.83 | 113 | MN |
| 5 | 1036 | 0.81 | 0.83 | 103 | empty |
Interfaces
7 interfaces between chains.
- A–D · 2207 Ų buried · 45 hydrogen bonds · protein-protein
- B–C · 2203 Ų buried · 48 hydrogen bonds · protein-protein
- C–D · 687 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 684 Ų buried · 10 hydrogen bonds · protein-protein
- E–F · 662 Ų buried · 8 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 1M35 · PDBe 1M35 · UniProt P15034
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