MolNFT v1 · #121713 · protein
Structure-function studies on role of hydrophobic clamping of a basic glutamate in catalysis by triosephosphate isomerase
5I3J · Triosephosphate isomerase, glycosomal: “Structure-function studies on role of hydrophobic clamping of a basic glutamate in catalysis by…”. X-ray diffraction, 1 ligand (NA), 3 pockets (best druggability 0.53). MolNFT v1 #121713 on…
- PDB
- 5I3J
- Type
- protein
- Length
- 498 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase, glycosomal
- EC
- 5.3.1.1
- UniProt
- P04789
- Ligands
- NA
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Triosephosphate isomerase, glycosomal (EC 5.3.1.1) | protein | 249 | 46% helix, 17% strand | P04789 |
Ligands and binding sites
- NA · Sodium ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.53 | 0.81 | 31 | empty |
| 2 | 116 | 0.52 | 0.82 | 27 | empty |
| 3 | 145 | 0.43 | 0.75 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 1569 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 5I3J · Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in… · the same entry in another collection · chain A against A, TM-score 1.00
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 0.99
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A 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 P04789
- Elsewhere: RCSB PDB 5I3J · PDBe 5I3J · UniProt P04789
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.