Research workbench
Trypanosoma cruzi trans-sialidase in complex with 2,3-difluorosialic acid (covalent intermediate)
Analyse Trypanosoma cruzi trans-sialidase in complex with 2,3-difluorosialic acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AH2
- Type
- protein
- Length
- 624 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trans-sialidase
- EC
- 3.2.1.18
- UniProt
- Q26966
- Ligands
- FSI, CL
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trans-sialidase (EC 3.2.1.18) | protein | 624 | 8% helix, 47% strand | Q26966 |
Ligands and binding sites
- FSI · 5-acetamido-3,5-dideoxy-3-fluoro-D-erythro-alpha-L-manno-non-2-ulopyranosonic acid · ligand · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · 3 copies · chains A
- IPA · Isopropyl alcohol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 216 | 0.64 | 0.83 | 34 | FSI, GOL |
| 2 | 262 | 0.56 | 0.77 | 24 | empty |
| 3 | 52 | 0.28 | 0.75 | 14 | empty |
| 4 | 66 | 0.27 | 0.72 | 19 | empty |
Modifications
Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).
Compared structures
- 2AH2 · Trypanosoma cruzi trans-sialidase in complex with 2,3-difluorosialic acid (covalent… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q26966
- Elsewhere: RCSB PDB 2AH2 · PDBe 2AH2 · UniProt Q26966
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