MolNFT v1 · #186422 · protein
Human triose phosphate isomerase Q181P
7RDE · Triosephosphate isomerase: “Human triose phosphate isomerase Q181P”. X-ray diffraction, 2 ligands (CA, BR), 1 pocket (best druggability 0.44). MolNFT v1 #186422 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7RDE
- Type
- protein
- Length
- 478 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1, 4.2.3.3
- UniProt
- P60174
- Ligands
- CA, BR
- Pockets
- 1 · best druggability 0.44
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, 4.2.3.3) | protein | 240 | 44% helix, 17% strand | P60174 |
| B | Triosephosphate isomerase (EC 5.3.1.1, 4.2.3.3) | protein | 238 | 44% helix, 17% strand | P60174 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.44 | 0.79 | 19 | BR |
Interfaces
1 interface between chains.
- A–B · 1755 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 7RDE · PDBe 7RDE · UniProt P60174
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