Research workbench
Dhna complex with 3-(5-amino-7-hydroxy-[1,2,3] triazolo [4,5- D]PYRIMIDIN-2-yl)-benzoic acid
Analyse Dhna complex with 3-(5-amino-7-hydroxy-[1,2,3] triazolo [4,5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RRI
- 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
- A45
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroneopterin aldolase (EC 4.1.2.25) | protein | 121 | 35% helix, 33% strand | P56740 |
Ligands and binding sites
- A45 · 3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-benzoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1RRI · DHNA complex with 3-(5-amino-7-hydroxy-[1,2,3] triazolo [4,5-d]pyrimidin-2-yl)-benzoic… · 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 1RRI · PDBe 1RRI · UniProt P56740
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