Research workbench
Ec-NMR structure of escherichia COLI maltose-binding protein determined by combining evolutionary couplings (ec) and sparse NMR data with a second set of rdc data simulated for an alternative alignment tensor. northeast structural genomics consortium target ER690
Analyse Ec-NMR structure of escherichia COLI maltose-binding protein determined by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N45
- Type
- protein
- Length
- 370 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic protein
- UniProt
- P0AEX9
- Pockets
- 2 · best druggability 0.79
Structure
solution nmr · 1 distinct chain · 43% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding periplasmic protein | protein | 370 | 43% helix, 14% strand | P0AEX9 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 704 | 0.79 | 0.83 | 67 | empty |
| 2 | 260 | 0.70 | 0.85 | 44 | empty |
Compared structures
- 2N45 · EC-NMR Structure of Escherichia coli Maltose-binding protein Determined by Combining… · the same entry in another collection · chain A against A, TM-score 1.00
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 P0AEX9
- Elsewhere: RCSB PDB 2N45 · PDBe 2N45 · UniProt P0AEX9
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