Research workbench
Malic enzyme from candidatus phytoplasma aywb in complex with NAD and MG2+
Analyse Malic enzyme from candidatus phytoplasma aywb in complex with NAD and MG2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CEE
- Type
- protein
- Length
- 387 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NAD-dependent malic enzyme
- EC
- 1.1.1.38
- UniProt
- Q2NK75
- Ligands
- NAD, MG
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent malic enzyme (EC 1.1.1.38) | protein | 387 | 47% helix, 13% strand | Q2NK75 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 543 | 0.62 | 0.75 | 44 | NAD |
| 2 | 83 | 0.33 | 0.74 | 17 | empty |
Compared structures
- 5CEE · Malic enzyme from Candidatus Phytoplasma AYWB in complex with NAD and Mg2+ · 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 Q2NK75
- Elsewhere: RCSB PDB 5CEE · PDBe 5CEE · UniProt Q2NK75
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