Research workbench
Atomic resolution crystal structure of E.COLI dihydroneopterin aldolase in complex with neopterin
Analyse Atomic resolution crystal structure of E.COLI dihydroneopterin aldolase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O90
- Type
- protein
- Length
- 115 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydroneopterin aldolase
- EC
- 4.1.2.25
- UniProt
- P0AC16
- Ligands
- NEU
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroneopterin aldolase (EC 4.1.2.25) | protein | 115 | 36% helix, 34% strand | P0AC16 |
Ligands and binding sites
- NEU · L-neopterin · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2O90 · Atomic resolution crystal structure of E.coli dihydroneopterin aldolase in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P0AC16 · AlphaFold monomer V2.0 prediction for dihydroneopterin aldolase (P0AC16) · 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 P0AC16
- Elsewhere: RCSB PDB 2O90 · PDBe 2O90 · UniProt P0AC16
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