Research workbench
E. COLI methylenetetrahydrofolate reductase (oxidized)
Analyse E. COLI methylenetetrahydrofolate reductase (oxidized) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZP3
- Type
- protein
- Length
- 841 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5,10-methylenetetrahydrofolate reductase
- EC
- 1.7.99.5
- UniProt
- P00394
- Ligands
- FAD, SO4
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 3 distinct chains · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5,10-methylenetetrahydrofolate reductase (EC 1.7.99.5) | protein | 284 | 49% helix, 13% strand | P00394 |
| B | 5,10-methylenetetrahydrofolate reductase (EC 1.7.99.5) | protein | 290 | 49% helix, 14% strand | P00394 |
| C | 5,10-methylenetetrahydrofolate reductase (EC 1.7.99.5) | protein | 267 | 49% helix, 15% strand | P00394 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 3 copies · chains A, B, C
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 627 | 0.76 | 0.82 | 73 | empty |
| 2 | 665 | 0.74 | 0.80 | 54 | FAD, MPD |
| 3 | 632 | 0.74 | 0.80 | 54 | FAD, MPD |
| 4 | 580 | 0.73 | 0.81 | 52 | FAD, MPD |
| 5 | 55 | 0.53 | 0.88 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1359 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 624 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 183 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1ZP3 · E. coli Methylenetetrahydrofolate Reductase (oxidized) · the same entry in another collection · 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 P00394
- Elsewhere: RCSB PDB 1ZP3 · PDBe 1ZP3 · UniProt P00394
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