Research workbench
NMR solution structure of ALG13 --- obtained with iterative cs-rosetta from backbone NMR data.
Analyse NMR solution structure of ALG13 --- obtained with iterative cs-rosetta from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KS6
- Type
- protein
- Length
- 201 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine transferase subunit ALG13
- EC
- 2.4.1.141
- UniProt
- P53178
- Pockets
- 1 · best druggability 0.38
Structure
solution nmr · 1 distinct chain · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine transferase subunit ALG13 (EC 2.4.1.141) | protein | 201 | 40% helix, 20% strand | P53178 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.38 | 0.78 | 16 | empty |
Compared structures
- 2KS6 · NMR solution structure of ALG13 --- obtained with iterative CS-Rosetta from backbone NMR… · the same entry in another collection · chain A against A, TM-score 1.00
- P53178 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine transferase subunit ALG13… · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P53178
- Elsewhere: RCSB PDB 2KS6 · PDBe 2KS6 · UniProt P53178
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