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Mutant R1617Q of the dihydroorotase domain of human CAD protein bound to the substrate carbamoyl aspartate

Analyse Mutant R1617Q of the dihydroorotase domain of human CAD protein bound to the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8PBH
Type: protein
Length: 362 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.87
Source: Homo sapiens
Molecule: CAD protein
EC: 6.3.5.5, 2.1.3.2, 3.5.2.3
UniProt: P27708
Ligands: NCD, ZN, NA
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · resolution 1.87 · 1 distinct chain · 35% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CAD protein (EC 6.3.5.5, 2.1.3.2, 3.5.2.3)	protein	362	35% helix, 20% strand	P27708

Ligands and binding sites

NCD · N-carbamoyl-L-aspartate · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains A
NA · Sodium ion · metal · chains A
FMT · Formic acid · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	76	0.41	0.79	15	empty
2	63	0.34	0.77	17	FMT

Modifications

Observed in the structure: 1 modified (carboxylation).

Compared structures

P27708 · AlphaFold monomer V2.0 prediction for cad protein (P27708) · 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 P27708
Elsewhere: RCSB PDB 8PBH · PDBe 8PBH · UniProt P27708

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