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Crystal structure of glyceraldehyde-3-phosphate DEHYDROGENASE1 from escherichia COLI at 2.09 ångström resolution
Analyse Crystal structure of glyceraldehyde-3-phosphate DEHYDROGENASE1 from escherichia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C5H
- Type
- protein
- Length
- 1,332 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A140NCK4
- Ligands
- NAD, PO4, CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| O, P, Q, R | — | protein | 333 | — | A0A140NCK4 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains O, P, Q, R
- PO4 · Phosphate ion · ion · 9 copies · chains O, P, Q, R
- CL · Chloride ion · ion · 7 copies · chains O, P, Q, R
- EDO · 1,2-ethanediol · additive · 6 copies · chains O, P, Q, R
- PEG · Di(hydroxyethyl)ether · additive · chains P
- GOL · Glycerol · additive · chains Q
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7C5H · Crystal Structure of Glyceraldehyde-3-phosphate dehydrogenase1 from Escherichia coli at… · the same entry in another collection · chain O against O, 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 A0A140NCK4
- Elsewhere: RCSB PDB 7C5H · PDBe 7C5H · UniProt A0A140NCK4
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