Research workbench
Structure of triosephosphate isomerase wild type human enzyme.
Analyse Structure of triosephosphate isomerase wild type human enzyme. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4POC
- Type
- protein
- Length
- 493 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- P60174
- Ligands
- K, NA, BR, PO4
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1) | protein | 246 | 44% helix, 16% strand | P60174 |
| B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 247 | 45% helix, 17% strand | P60174 |
Ligands and binding sites
- K · Potassium ion · metal · 2 copies · chains A, B
- NA · Sodium ion · metal · chains A
- BR · Bromide ion · ion · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · chains 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 | 50 | 0.65 | 0.96 | 15 | empty |
| 2 | 58 | 0.37 | 0.79 | 24 | PO4, BR |
| 3 | 58 | 0.36 | 0.78 | 16 | empty |
| 4 | 54 | 0.34 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1779 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
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 P60174
- Elsewhere: RCSB PDB 4POC · PDBe 4POC · UniProt P60174
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