MolNFT v1 · #146328 · protein
Crystal structure of bifunctional enzyme fold- methylenetetrahydrofolate DEHYDROGENASE/CYCLOHYDROLASE from campylobacter jejuni
6DE8: “Crystal structure of bifunctional enzyme fold- methylenetetrahydrofolate DEHYDROGENASE/CYCLOHYDROLASE from…”. X-ray diffraction, 3 ligands (K, IOD, CL). MolNFT v1 #146328 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6DE8
- Type
- protein
- Length
- 564 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q0PA35
- Ligands
- K, IOD, CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 282 | — | Q0PA35 |
Ligands and binding sites
- K · Potassium ion · metal · chains B
- IOD · Iodide ion · ion · 17 copies · chains A, B
- CL · Chloride ion · ion · chains B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6DE8 · Crystal Structure of Bifunctional Enzyme FolD-Methylenetetrahydrofolate… · the same entry in another collection · chain A against A, TM-score 1.00
- Q0PA35 · AlphaFold monomer V2.0 prediction for bifunctional protein fold (Q0PA35) · 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 Q0PA35
- Elsewhere: RCSB PDB 6DE8 · PDBe 6DE8 · UniProt Q0PA35
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