Research workbench
Solution NMR structure of protein ytfp from escherichia COLI. northeast structural genomics consortium target ER111.
Analyse Solution NMR structure of protein ytfp from escherichia COLI. northeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XHS
- Type
- protein
- Length
- 113 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical UPF0131 protein ytfp
- UniProt
- P39323
- Pockets
- 1 · best druggability 0.58
Structure
solution nmr · 1 distinct chain · 13% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical UPF0131 protein ytfp | protein | 113 | 13% helix, 48% strand | P39323 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 227 | 0.58 | 0.79 | 22 | empty |
Compared structures
- 1XHS · Solution NMR Structure of Protein ytfP from Escherichia coli. Northeast Structural… · 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 P39323
- Elsewhere: RCSB PDB 1XHS · PDBe 1XHS · UniProt P39323
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.