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Crystal structure of T4-bacteriophage deoxycytidylate deaminase, mutant R115E

Analyse Crystal structure of T4-bacteriophage deoxycytidylate deaminase, mutant R115E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VQ2
Type: protein
Length: 173 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deoxycytidylate deaminase
EC: 3.5.4.12
UniProt: P16006
Ligands: DDN, ZN
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deoxycytidylate deaminase (EC 3.5.4.12)	protein	173	39% helix, 23% strand	P16006

Ligands and binding sites

DDN · 3,4-dihydro-2'-deoxyuridine-5'-monophosphate · ligand · chains A
ZN · Zinc ion · metal · 2 copies · 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	128	0.64	0.88	24	DDN

Compared structures

1VQ2 · Crystal structure of T4-bacteriophage deoxycytidylate deaminase, mutant R115E · 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 P16006
Elsewhere: RCSB PDB 1VQ2 · PDBe 1VQ2 · UniProt P16006

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