Research workbench
Crystal structure of mes buffer bound form of glyceraldehyde 3- phosphate dehydrogenase from escherichia COLI
Analyse Crystal structure of mes buffer bound form of glyceraldehyde 3- phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1S7C
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glyceraldehyde 3-phosphate dehydrogenase a
- EC
- 1.2.1.12
- UniProt
- P0A9B2
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glyceraldehyde 3-phosphate dehydrogenase a (EC 1.2.1.12) | protein | 330 | 30% helix, 27% strand | P0A9B2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 406 | 0.60 | 0.76 | 48 | SO4, MES |
| 2 | 53 | 0.37 | 0.80 | 13 | empty |
| 3 | 76 | 0.34 | 0.75 | 13 | empty |
| 4 | 53 | 0.31 | 0.76 | 14 | empty |
Compared structures
- 1S7C · Crystal structure of MES buffer bound form of glyceraldehyde 3-phosphate dehydrogenase… · 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 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 P0A9B2
- Elsewhere: RCSB PDB 1S7C · PDBe 1S7C · UniProt P0A9B2
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