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Arabidopsis aspartate transcarbamoylase mutant F161A complex with ump

Analyse Arabidopsis aspartate transcarbamoylase mutant F161A complex with ump in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6YWJ
Type: protein
Length: 623 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyrb
UniProt: A0A178VJE3
Ligands: U5P
Pockets: 8 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pyrb	protein	312	42% helix, 14% strand	A0A178VJE3
B	Pyrb	protein	311	43% helix, 15% strand	A0A178VJE3

Ligands and binding sites

U5P · Uridine-5'-monophosphate · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	385	0.64	0.79	40	U5P
2	406	0.64	0.78	42	U5P
3	215	0.63	0.82	30	empty
4	149	0.59	0.83	31	empty
5	133	0.57	0.83	20	empty

Interfaces

1 interface between chains.

A–B · 924 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6YWJ · Arabidopsis aspartate transcarbamoylase mutant F161A complex with UMP · 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 A0A178VJE3
Elsewhere: RCSB PDB 6YWJ · PDBe 6YWJ · UniProt A0A178VJE3

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