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Crystal structure of human aspartate beta-hydroxylase isoform a

Analyse Crystal structure of human aspartate beta-hydroxylase isoform a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5APA
Type: protein
Length: 196 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.05
Source: HOMO SAPIENS
Molecule: ASPARTYL/ASPARAGINYL beta-hydroxylase
EC: 1.14.11.16
UniProt: Q12797
Ligands: LMR, NI

Structure

x-ray diffraction · resolution 2.05 · 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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