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Crystal structure of a putative transcarbamoylase from enterococcus faecalis

Analyse Crystal structure of a putative transcarbamoylase from enterococcus faecalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YFK
Type: protein
Length: 771 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ASPARTATE/ORNITHINE carbamoyltransferase
EC: 2.1.3.-
UniProt: C7YCV8
Pockets: 5 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ASPARTATE/ORNITHINE carbamoyltransferase (EC 2.1.3.-)	protein	385	52% helix, 15% strand	C7YCV8
B	ASPARTATE/ORNITHINE carbamoyltransferase (EC 2.1.3.-)	protein	386	51% helix, 14% strand	C7YCV8

Pockets

5 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	283	0.59	0.78	44	empty
2	108	0.46	0.79	14	empty
3	87	0.45	0.80	13	empty
4	149	0.43	0.75	24	empty
5	187	0.42	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 71 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2YFK · Crystal structure of a putative transcarbamoylase from Enterococcus faecalis · 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 C7YCV8
Elsewhere: RCSB PDB 2YFK · PDBe 2YFK · UniProt C7YCV8

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