Research workbench
Structural analysis of glyceraldehyde 3-phosphate dehydrogenase from escherichia COLI: direct evidence for substrate binding and cofactor-induced conformational changes
Analyse Structural analysis of glyceraldehyde 3-phosphate dehydrogenase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DC3
- Type
- protein
- Length
- 660 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glyceraldehyde 3-phosphate dehydrogenase
- EC
- 1.2.1.12
- UniProt
- P0A9B2
- Pockets
- 7 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) | protein | 330 | 30% helix, 27% strand | P0A9B2 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 399 | 0.60 | 0.76 | 46 | empty |
| 2 | 398 | 0.60 | 0.76 | 44 | empty |
| 3 | 68 | 0.33 | 0.75 | 13 | empty |
| 4 | 63 | 0.32 | 0.76 | 13 | empty |
| 5 | 81 | 0.32 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2001 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 1DC3 · Structural analysis of glyceraldehyde 3-phosphate dehydrogenase from escherichia COLI… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A9B2 · AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase a (P0A9B2) · 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 P0A9B2
- Elsewhere: RCSB PDB 1DC3 · PDBe 1DC3 · UniProt P0A9B2
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