MolNFT v1 · #113771 · protein
Crystal structure of human aspartate beta-hydroxylase isoform a
5APA · ASPARTYL/ASPARAGINYL beta-hydroxylase: “Crystal structure of human aspartate beta-hydroxylase isoform a”. X-ray diffraction, 2 ligands (LMR, NI). MolNFT v1 #113771 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5APA
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ASPARTYL/ASPARAGINYL beta-hydroxylase
- EC
- 1.14.11.16
- UniProt
- Q12797
- Ligands
- LMR, NI
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ASPARTYL/ASPARAGINYL beta-hydroxylase (EC 1.14.11.16) | protein | 196 | 24% helix, 34% strand | Q12797 |
Ligands and binding sites
- LMR · (2S)-2-hydroxybutanedioic acid · ligand · chains A
- NI · Nickel (II) ion · metal · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5APA · Crystal structure of human aspartate beta-hydroxylase isoform a · the same entry in another collection · chain A against A, TM-score 1.00
- Q12797 · AlphaFold monomer V2.0 prediction for ASPARTYL/ASPARAGINYL beta- hydroxylase (Q12797) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q12797
- Elsewhere: RCSB PDB 5APA · PDBe 5APA · UniProt Q12797
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