Research workbench
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from chlamydia trachomatis with bound NAD
Analyse Crystal structure of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OK4
- Type
- protein
- Length
- 1,335 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0CE13
- Ligands
- NAD, PO4, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | — | protein | 334 | — | P0CE13 |
| B | — | protein | 333 | — | P0CE13 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, C, B, D
- PO4 · Phosphate ion · ion · 6 copies · chains A, B, C, D
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 15 copies · chains A, B, D, C
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6OK4 · Crystal Structure of Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Chlamydia… · the same entry in another collection · chain D against D, TM-score 1.00
- P0CE13 · AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (P0CE13) · a predicted model of the same protein · chain B 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 P0CE13
- Elsewhere: RCSB PDB 6OK4 · PDBe 6OK4 · UniProt P0CE13
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.