MolNFT v1 · #16034 · protein
MBP-L30
1NMU · Maltose-binding periplasmic protein: “MBP-L30”. X-ray diffraction, 1 ligand (GLC), 11 pockets (best druggability 0.74). MolNFT v1 #16034 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1NMU
- Type
- protein
- Length
- 943 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic protein; 60S ribosomal protein L30
- UniProt
- P02928, P14120
- Ligands
- GLC
- Pockets
- 11 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Maltose-binding periplasmic protein | protein | 368 | 45% helix, 21% strand | P02928 |
| B | 60S ribosomal protein L30 | protein | 104 | 46% helix, 18% strand | P14120 |
| D | 60S ribosomal protein L30 | protein | 103 | 40% helix, 17% strand | P14120 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1097 | 0.74 | 0.77 | 87 | empty |
| 2 | 741 | 0.74 | 0.79 | 55 | GLC |
| 3 | 368 | 0.72 | 0.84 | 31 | GLC |
| 4 | 243 | 0.50 | 0.75 | 34 | empty |
| 5 | 119 | 0.46 | 0.79 | 37 | empty |
Interfaces
4 interfaces between chains.
- B–C · 741 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 371 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 339 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 298 Ų buried · 3 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 P02928
- Every structure of UniProt P14120
- Elsewhere: RCSB PDB 1NMU · PDBe 1NMU · UniProt P02928 · UniProt P14120
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