MolNFT v1 · #147429 · protein
The human methylenetetrahydrofolate DEHYDROGENASE/CYCLOHYDROLASE (fold) complexed with NADP
6ECR: “The human methylenetetrahydrofolate DEHYDROGENASE/CYCLOHYDROLASE (fold) complexed with NADP”. X-ray diffraction, 1 ligand (NAP). MolNFT v1 #147429 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6ECR
- Type
- protein
- Length
- 580 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11586
- Ligands
- NAP
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 285 | — | P11586 |
| B | — | protein | 295 | — | P11586 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- ACT · Acetate ion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6ECR · The human methylenetetrahydrofolate dehydrogenase/cyclohydrolase (FolD) complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P11586 · AlphaFold monomer V2.0 prediction for C-1-tetrahydrofolate synthase, cytoplasmic (P11586) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P11586
- Elsewhere: RCSB PDB 6ECR · PDBe 6ECR · UniProt P11586
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