MolNFT v1 · #45472 · protein
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
2N45: “Ec-NMR structure of escherichia COLI maltose-binding protein determined by combining evolutionary couplings…”. Solution nmr. MolNFT v1 #45472 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2N45
- Type
- protein
- Length
- 370 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AEX9
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 370 | — | P0AEX9 |
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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