Research workbench
Dhna complex with 8-amino-1,3-dimethyl-3,7-dihydropurine-2,6-dione
Analyse Dhna complex with 8-amino-1,3-dimethyl-3,7-dihydropurine-2,6-dione in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RS2
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydroneopterin aldolase
- EC
- 4.1.2.25
- UniProt
- P56740
- Ligands
- 209
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroneopterin aldolase (EC 4.1.2.25) | protein | 121 | 35% helix, 31% strand | P56740 |
Ligands and binding sites
- 209 · 8-amino-1,3-dimethyl-3,7-dihydropurine-2,6-dione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1RS2 · DHNA complex with 8-Amino-1,3-dimethyl-3,7-dihydropurine-2,6-dione · the same entry in another collection · chain A against A, TM-score 1.00
- P56740 · AlphaFold monomer V2.0 prediction for dihydroneopterin aldolase (P56740) · 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 P56740
- Elsewhere: RCSB PDB 1RS2 · PDBe 1RS2 · UniProt P56740
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