Research workbench
Crystal structure of triosephosphate isomerase from stenotrophomonas maltophilia K279A
Analyse Crystal structure of triosephosphate isomerase from stenotrophomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6W4U
- Type
- protein
- Length
- 505 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- B2FNY1
- Ligands
- NA, CL
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1) | protein | 252 | 47% helix, 14% strand | B2FNY1 |
| B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 253 | 46% helix, 15% strand | B2FNY1 |
Ligands and binding sites
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 | 448 | 0.68 | 0.80 | 44 | CL |
| 2 | 152 | 0.45 | 0.76 | 36 | empty |
| 3 | 139 | 0.44 | 0.76 | 29 | empty |
| 4 | 50 | 0.31 | 0.77 | 13 | empty |
| 5 | 53 | 0.26 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1546 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 6W4U · Crystal structure of Triosephosphate isomerase from Stenotrophomonas maltophilia K279a · the same entry in another collection · chain A against A, TM-score 1.00
- B2FNY1 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (B2FNY1) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 B2FNY1
- Elsewhere: RCSB PDB 6W4U · PDBe 6W4U · UniProt B2FNY1
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