Research workbench
Glutamate mutase (B12-binding subunit), NMR, minimized average structure
Analyse Glutamate mutase (B12-binding subunit), NMR, minimized average structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BE1
- Type
- protein
- Length
- 137 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate mutase
- EC
- 5.4.99.1
- UniProt
- Q05488
- Pockets
- 1 · best druggability 0.46
Structure
solution nmr · 1 distinct chain · 21% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate mutase (EC 5.4.99.1) | protein | 137 | 21% helix, 19% strand | Q05488 |
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 | 65 | 0.46 | 0.83 | 16 | empty |
Compared structures
- 1BE1 · Glutamate mutase (B12-binding subunit), NMR, minimized average structure · the same entry in another collection · chain A against A, TM-score 1.00
- Q05488 · AlphaFold monomer V2.0 prediction for glutamate mutase sigma subunit (Q05488) · a predicted model of the same protein · chain A against A, TM-score 0.66
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 Q05488
- Elsewhere: RCSB PDB 1BE1 · PDBe 1BE1 · UniProt Q05488
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