Research workbench
The crystal structure of human MACROD2 in space group P41212
Analyse The crystal structure of human MACROD2 in space group P41212 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Y4Y
- Type
- protein
- Length
- 864 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AA25, A1Z1Q3
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 214 | — | P0AA25, A1Z1Q3 |
| B | — | protein | 215 | — | P0AA25, A1Z1Q3 |
| C | — | protein | 218 | — | P0AA25, A1Z1Q3 |
| D | — | protein | 217 | — | P0AA25, A1Z1Q3 |
Ligands and binding sites
- TLA · L(+)-tartaric acid · additive · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6Y4Y · The crystal structure of human MACROD2 in space group P41212 · the same entry in another collection · chain D against D, TM-score 1.00
- A1Z1Q3 · AlphaFold monomer V2.0 prediction for ADP-ribose glycohydrolase MACROD2 (A1Z1Q3) · 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 P0AA25
- Every structure of UniProt A1Z1Q3
- Elsewhere: RCSB PDB 6Y4Y · PDBe 6Y4Y · UniProt P0AA25 · UniProt A1Z1Q3
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