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Northeast structural genomics consortium (nesg id TT50) structure of MTH169, the purs subunit of fgam synthetase
Analyse Northeast structural genomics consortium (nesg id TT50) structure of MTH169… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GTD
- Type
- protein
- Length
- 165 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MTH169
- UniProt
- O26271
- Pockets
- 2 · best druggability 0.29
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MTH169 | protein | 81 | 36% helix, 38% strand | O26271 |
| B | MTH169 | protein | 84 | 35% helix, 39% strand | O26271 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.29 | 0.74 | 13 | empty |
| 2 | 51 | 0.28 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1248 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 1GTD · Northeast structural genomics consortium (nesg id TT50) structure of MTH169, the purs… · the same entry in another collection · chain A against A, TM-score 1.00
- O26271 · AlphaFold monomer V2.0 prediction for phosphoribosylformylglycinamidine synthase subunit… · a predicted model of the same protein · chain A against A, TM-score 0.87
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 O26271
- Elsewhere: RCSB PDB 1GTD · PDBe 1GTD · UniProt O26271
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