Research workbench
S96P change is a second-site suppressor for H95N sluggish mutant triosephosphate isomerase
Analyse S96P change is a second-site suppressor for H95N sluggish mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TPV
- Type
- protein
- Length
- 490 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- P00940
- Ligands
- PGH
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 245 | 45% helix, 18% strand | P00940 |
Ligands and binding sites
- PGH · Phosphoglycolohydroxamic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.71 | 0.96 | 24 | empty |
| 2 | 58 | 0.41 | 0.81 | 21 | PGH |
| 3 | 51 | 0.39 | 0.81 | 19 | PGH |
| 4 | 67 | 0.37 | 0.78 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1679 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 1TPV · S96P change is a second-site suppressor for H95N sluggish mutant triosephosphate isomerase · the same entry in another collection · chain A against A, TM-score 1.00
- P00940 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P00940) · 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 P00940
- Elsewhere: RCSB PDB 1TPV · PDBe 1TPV · UniProt P00940
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