Research workbench
Crystal structure of galactitol-1-phosphate dehydrogenase from escherichia COLI
Analyse Crystal structure of galactitol-1-phosphate dehydrogenase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A2C
- Type
- protein
- Length
- 692 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galactitol-1-phosphate 5-dehydrogenase
- EC
- 1.1.1.251
- UniProt
- P0A9S3
- Ligands
- NI, ZN
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Galactitol-1-phosphate 5-dehydrogenase (EC 1.1.1.251) | protein | 346 | 32% helix, 26% strand | P0A9S3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.79 | 0.99 | 18 | empty |
| 2 | 850 | 0.73 | 0.78 | 78 | NI |
| 3 | 650 | 0.73 | 0.80 | 62 | NI |
| 4 | 157 | 0.46 | 0.76 | 21 | empty |
| 5 | 152 | 0.41 | 0.74 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 1820 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 4A2C · Crystal structure of galactitol-1-phosphate dehydrogenase from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P0A9S3 · AlphaFold monomer V2.0 prediction for galactitol 1-phosphate 5-dehydrogenase (P0A9S3) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P0A9S3
- Elsewhere: RCSB PDB 4A2C · PDBe 4A2C · UniProt P0A9S3
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