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Crystal structure of E. COLI aspartate transcarbamoylase K164E/E239K mutant in an intermediate state

Analyse Crystal structure of E. COLI aspartate transcarbamoylase K164E/E239K mutant in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4E2F
Type: protein
Length: 2,724 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartate carbamoyltransferase catalytic chain; Aspartate carbamoyltransferase regulatory…
EC: 2.1.3.2
UniProt: P0A786, P0A7F3
Ligands: ZN
Pockets: 20 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
I, K, G, C, A, E	Aspartate carbamoyltransferase catalytic chain (EC 2.1.3.2)	protein	310	40% helix, 16% strand	P0A786
D, B, J, L, H, F	Aspartate carbamoyltransferase regulatory chain	protein	144	12% helix, 38% strand	P0A7F3

Ligands and binding sites

ZN · Zinc ion · metal · 6 copies · chains D, B, J, L, H, F

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

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	743	0.85	0.88	66	empty
2	851	0.84	0.87	78	empty
3	438	0.74	0.84	66	empty
4	601	0.73	0.81	64	empty
5	866	0.73	0.78	90	empty

Interfaces

29 interfaces between chains.

K–G · 904 Å² buried · 6 hydrogen bonds · protein-protein
K–C · 881 Å² buried · 10 hydrogen bonds · protein-protein
G–C · 878 Å² buried · 6 hydrogen bonds · protein-protein
I–A · 868 Å² buried · 7 hydrogen bonds · protein-protein
I–E · 862 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

4E2F · Crystal Structure of E. coli Aspartate Transcarbamoylase K164E/E239K Mutant in an… · the same entry in another collection · chain F against F, 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 4E2F · PDBe 4E2F · UniProt P0A786 · UniProt P0A7F3

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