Research workbench

Xcogt in complex with C-udp

Analyse Xcogt in complex with C-udp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XGS
Type: protein
Length: 1,021 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xcogt
UniProt: Q8PC69
Ligands: 44P
Pockets: 6 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xcogt	protein	542	53% helix, 10% strand	Q8PC69
B	Xcogt	protein	479	49% helix, 12% strand	Q8PC69

Ligands and binding sites

44P · 5'-O-[(S)-hydroxy(phosphonomethyl)phosphoryl]uridine · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	411	0.72	0.83	58	44P
2	315	0.69	0.83	36	44P
3	193	0.58	0.81	32	empty
4	121	0.53	0.82	23	empty
5	201	0.50	0.76	34	empty

Interfaces

1 interface between chains.

A–B · 622 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2XGS · XcOGT in complex with C-UDP · 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 Q8PC69
Elsewhere: RCSB PDB 2XGS · PDBe 2XGS · UniProt Q8PC69

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