MolNFT v1 · #12116 · protein

The structure of escherichia COLI cytosine deaminase bound to 4- hydroxy-3,4-dihydro-1H-pyrimidin-2-one

1K70: “The structure of escherichia COLI cytosine deaminase bound to 4- hydroxy-3,4-dihydro-1H-pyrimidin-2-one”. X-ray diffraction, 2 ligands (HPY, FE), 3 pockets (best druggability 0.35). MolNFT v1 #12116 on GenesisL1: 3D structure…

PDB: 1K70
Type: protein
Length: 423 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytosine deaminase
EC: 3.5.4.1
UniProt: P25524
Ligands: HPY, FE
Pockets: 3 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytosine deaminase (EC 3.5.4.1)	protein	423	37% helix, 23% strand	P25524

Ligands and binding sites

HPY · 4-hydroxy-3,4-dihydro-1H-pyrimidin-2-one · ligand · chains A
FE · Fe (III) ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	75	0.35	0.76	22	empty
2	52	0.30	0.76	12	empty
3	71	0.28	0.72	19	empty

Compared structures

1K70 · The Structure of Escherichia coli Cytosine Deaminase bound to… · the same entry in another collection · chain A against A, TM-score 1.00
P25524 · AlphaFold monomer V2.0 prediction for cytosine deaminase (P25524) · a predicted model of the same protein · 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 P25524
Elsewhere: RCSB PDB 1K70 · PDBe 1K70 · UniProt P25524

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