Research workbench
X-ray crystal structure of tyrosine aminomutase from streptomyces globisporus
Analyse X-ray crystal structure of tyrosine aminomutase from streptomyces globisporus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OHY
- Type
- protein
- Length
- 1,053 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine aminomutase
- EC
- 5.4.3.6
- UniProt
- Q8GMG0
- Pockets
- 9 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine aminomutase (EC 5.4.3.6) | protein | 526 | 56% helix, 7% strand | Q8GMG0 |
| B | Tyrosine aminomutase (EC 5.4.3.6) | protein | 527 | 57% helix, 7% strand | Q8GMG0 |
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 174 | 0.55 | 0.80 | 44 | empty |
| 2 | 84 | 0.42 | 0.79 | 21 | empty |
| 3 | 74 | 0.39 | 0.79 | 16 | empty |
| 4 | 104 | 0.39 | 0.76 | 21 | empty |
| 5 | 81 | 0.35 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 4952 Ų buried · 90 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 2OHY · X-ray Crystal Structure of Tyrosine Aminomutase from streptomyces globisporus · the same entry in another collection · chain B against B, TM-score 1.00
- Q8GMG0 · AlphaFold monomer V2.0 prediction for mio-dependent tyrosine 2,3-aminomutase (Q8GMG0) · a predicted model of the same protein · 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 Q8GMG0
- Elsewhere: RCSB PDB 2OHY · PDBe 2OHY · UniProt Q8GMG0
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