Research workbench

Atcase Y165F mutant

Analyse Atcase Y165F mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 9ATC
Type: protein
Length: 456 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartate transcarbamoylase
EC: 2.1.3.2
UniProt: P0A786, P0A7F3
Ligands: ZN
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aspartate transcarbamoylase (EC 2.1.3.2)	protein	310	36% helix, 15% strand	P0A786
B	Aspartate transcarbamoylase (EC 2.1.3.2)	protein	146	14% helix, 17% strand	P0A7F3

Ligands and binding sites

ZN · Zinc ion · metal · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	130	0.63	0.86	26	empty
2	350	0.58	0.76	40	empty
3	176	0.44	0.74	22	empty
4	94	0.38	0.76	18	empty

Interfaces

1 interface between chains.

A–B · 652 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

9ATC · Atcase Y165F mutant · the same entry in another collection · chain A against A, TM-score 1.00

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 P0A786
Every structure of UniProt P0A7F3
Elsewhere: RCSB PDB 9ATC · PDBe 9ATC · UniProt P0A786 · UniProt P0A7F3

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