Research workbench
Offset of a catalytic lesion by a bound water soluble
Analyse Offset of a catalytic lesion by a bound water soluble in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TPB
- 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
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1, 2 | Triosephosphate isomerase (EC 5.3.1.1) | protein | 245 | 45% helix, 16% strand | P00940 |
Ligands and binding sites
- PGH · Phosphoglycolohydroxamic acid · ligand · 2 copies · chains 1, 2
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.71 | 0.96 | 25 | empty |
| 2 | 60 | 0.42 | 0.82 | 24 | PGH |
| 3 | 64 | 0.37 | 0.79 | 20 | empty |
Interfaces
1 interface between chains.
- 1–2 · 1705 Ų buried · 32 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 P00940
- Elsewhere: RCSB PDB 1TPB · PDBe 1TPB · UniProt P00940
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