Research workbench
Fructose-1,6-bisphosphate ALDOLASE/PHOSPHATASE from thermoproteus neutrophilus, dhap-bound form
Analyse Fructose-1,6-bisphosphate ALDOLASE/PHOSPHATASE from thermoproteus neutrophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3T2C
- Type
- protein
- Length
- 389 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-1,6-bisphosphate ALDOLASE/PHOSPHATASE
- EC
- 4.1.2.13, 3.1.3.11
- UniProt
- B1YAL1
- Ligands
- 13P, MG
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-1,6-bisphosphate ALDOLASE/PHOSPHATASE (EC 4.1.2.13, 3.1.3.11) | protein | 389 | 31% helix, 28% strand | B1YAL1 |
Ligands and binding sites
- 13P · 1,3-dihydroxyacetonephosphate · ligand · 2 copies · chains A
- MG · Magnesium ion · metal · 3 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 139 | 0.49 | 0.78 | 21 | empty |
| 2 | 107 | 0.46 | 0.79 | 16 | empty |
| 3 | 50 | 0.28 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 3T2C · Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus… · the same entry in another collection · chain A against A, TM-score 1.00
- B1YAL1 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphate ALDOLASE/PHOSPHATASE… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 B1YAL1
- Elsewhere: RCSB PDB 3T2C · PDBe 3T2C · UniProt B1YAL1
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