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Evolution of chlorella virus dutpase

Analyse Evolution of chlorella virus dutpase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3C2T
Type: protein
Length: 249 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deoxyuridine triphosphatase
EC: 3.6.1.23
UniProt: Q5I3E5
Ligands: DUD, MG
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deoxyuridine triphosphatase (EC 3.6.1.23)	protein	125	6% helix, 41% strand	Q5I3E5
B	Deoxyuridine triphosphatase (EC 3.6.1.23)	protein	124	6% helix, 40% strand	Q5I3E5

Ligands and binding sites

DUD · Deoxyuridine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	157	0.50	0.78	28	empty

Interfaces

1 interface between chains.

A–B · 332 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

3C2T · Evolution of chlorella virus dUTPase · 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 Q5I3E5
Elsewhere: RCSB PDB 3C2T · PDBe 3C2T · UniProt Q5I3E5

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