MolNFT v1 · #21924 · protein
Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase
1SPQ: “Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase”. X-ray diffraction, 5 pockets (best druggability 0.73). MolNFT v1 #21924 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1SPQ
- Type
- protein
- Length
- 482 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
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1) | protein | 243 | 44% helix, 16% strand | P00940 |
| B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 239 | 44% helix, 17% strand | P00940 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.73 | 0.96 | 25 | empty |
| 2 | 113 | 0.49 | 0.80 | 21 | empty |
| 3 | 113 | 0.42 | 0.76 | 28 | empty |
| 4 | 50 | 0.37 | 0.81 | 17 | PEG |
| 5 | 61 | 0.35 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1714 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 1SPQ · Understanding protein lids: Structural analysis of active hinge mutants in… · 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 B against A, TM-score 0.99
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 1SPQ · PDBe 1SPQ · UniProt P00940
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