MolNFT v1 · #151162 · protein

Human dihydroorotase mutant F1563T apo structure

6HFE · Cad protein: “Human dihydroorotase mutant F1563T apo structure”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.63). MolNFT v1 #151162 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6HFE
Type: protein
Length: 362 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cad protein
EC: 6.3.5.5, 2.1.3.2, 3.5.2.3
UniProt: P27708
Ligands: ZN
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 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

ZN · Zinc ion · metal · 4 copies · chains A
FMT · Formic acid · additive · 6 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	263	0.63	0.81	36	FMT
2	83	0.40	0.78	16	empty
3	55	0.32	0.77	17	FMT

Modifications

Observed in the structure: 1 modified (carboxylation).

Compared structures

6HFE · Human dihydroorotase mutant F1563T apo structure · the same entry in another collection · chain A against A, TM-score 1.00
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 6HFE · PDBe 6HFE · UniProt P27708

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