MolNFT v1 · #11840 · protein

Catalytic mechanism of CTP:PHOSPHOCHOLINE cytidylytransferase from streptococcus pneumoniae (licc)

1JYK: “Catalytic mechanism of CTP:PHOSPHOCHOLINE cytidylytransferase from streptococcus pneumoniae (licc)”. X-ray diffraction, 1 pocket (best druggability 0.68). MolNFT v1 #11840 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1JYK
Type: protein
Length: 229 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CTP:PHOSPHOCHOLINE cytidylytransferase
UniProt: Q97QE9
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CTP:PHOSPHOCHOLINE cytidylytransferase	protein	229	30% helix, 26% strand	Q97QE9

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	469	0.68	0.80	46	empty

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

1JYK · Catalytic Mechanism of CTP:phosphocholine Cytidylyltransferase from Streptococcus… · 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 Q97QE9
Elsewhere: RCSB PDB 1JYK · PDBe 1JYK · UniProt Q97QE9

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