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Structure of OHCU decarboxylase from zebrafish

Analyse Structure of OHCU decarboxylase from zebrafish in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O70
Type: protein
Length: 992 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.8
Source: Danio rerio
Molecule: OHCU decarboxylase
UniProt: A1L259
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · resolution 1.8 · 4 distinct chains · 70% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	OHCU decarboxylase	protein	165	70% helix, 0% strand	A1L259
B, D, E	OHCU decarboxylase	protein	164	70% helix, 0% strand	A1L259
C	OHCU decarboxylase	protein	167	70% helix, 0% strand	A1L259
F	OHCU decarboxylase	protein	168	69% helix, 0% strand	A1L259

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	696	0.71	0.78	71	empty
2	682	0.70	0.78	80	empty
3	432	0.64	0.78	53	empty
4	149	0.44	0.75	25	empty

Interfaces

5 interfaces between chains.

E–F · 1222 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 1196 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 1180 Å² buried · 15 hydrogen bonds · protein-protein
C–F · 419 Å² buried · 2 hydrogen bonds · protein-protein
A–C · 252 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2O70 · Structure of ohcu decarboxylase from zebrafish · the same entry in another collection · chain F against F, TM-score 1.00
A1L259 · AlphaFold monomer V2.0 prediction for 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline… · a predicted model of the same protein · chain B 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 A1L259
Elsewhere: RCSB PDB 2O70 · PDBe 2O70 · UniProt A1L259

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