MolNFT v2 · #216495 · protein

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

8PBH: “Mutant R1617Q of the dihydroorotase domain of human CAD protein bound to the substrate carbamoyl aspartate”. X-ray diffraction at 1.87, 3 ligands (NCD, ZN, NA), 2 pockets (best druggability 0.41). MolNFT v2 #216495 on GenesisL1: 3D…

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).

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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