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Chlorovirus pbcv-1 bi-functional DCMP/DCTP deaminase bi-dcd with DTTP/DTMP bound

Analyse Chlorovirus pbcv-1 bi-functional DCMP/DCTP deaminase bi-dcd with DTTP/DTMP bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7FH9
Type: protein
Length: 140 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CMP/DCMP-type deaminase domain-containing protein
UniProt: O41078
Ligands: TTP, TMP, ZN, MG
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CMP/DCMP-type deaminase domain-containing protein	protein	140	44% helix, 18% strand	O41078

Ligands and binding sites

TTP · Thymidine-5'-triphosphate · ligand · chains A
TMP · Thymidine-5'-phosphate · ligand · chains A
ZN · Zinc ion · metal · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	203	0.56	0.79	29	TMP

Compared structures

7FH9 · chlorovirus PBCV-1 bi-functional dCMP/dCTP deaminase bi-DCD with dTTP/dTMP bound · 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 O41078
Elsewhere: RCSB PDB 7FH9 · PDBe 7FH9 · UniProt O41078

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