MolNFT v1 · #113421 · protein
Crystal structure of saccharomyces cerevisiae MEP2
5AEX · Ammonium transporter MEP2: “Crystal structure of saccharomyces cerevisiae MEP2”. X-ray diffraction, 1 ligand (PO4), 20 pockets (best druggability 0.77). MolNFT v1 #113421 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5AEX
- Type
- protein
- Length
- 4,049 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ammonium transporter MEP2
- UniProt
- P41948
- Ligands
- PO4
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 5 distinct chains · 61% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, E, F | Ammonium transporter MEP2 | protein | 456 | 59% helix, 2% strand | P41948 |
| D | Ammonium transporter MEP2 | protein | 455 | 60% helix, 2% strand | P41948 |
| H | Ammonium transporter MEP2 | protein | 440 | 61% helix, 1% strand | P41948 |
| I | Ammonium transporter MEP2 | protein | 447 | 62% helix, 2% strand | P41948 |
| J | Ammonium transporter MEP2 | protein | 427 | 61% helix, 2% strand | P41948 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 9 copies · chains A, B, C, D, E, F, H, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 619 | 0.77 | 0.83 | 65 | empty |
| 2 | 596 | 0.76 | 0.83 | 75 | empty |
| 3 | 71 | 0.73 | 0.95 | 19 | empty |
| 4 | 443 | 0.72 | 0.82 | 71 | empty |
| 5 | 52 | 0.72 | 0.97 | 20 | empty |
Interfaces
15 interfaces between chains.
- B–C · 2390 Ų buried · 15 hydrogen bonds · protein-protein
- D–F · 2381 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 2365 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 2354 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 2354 Ų buried · 14 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 P41948
- Elsewhere: RCSB PDB 5AEX · PDBe 5AEX · UniProt P41948
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