MolNFT v1 · #11440 · protein

Crystal structure of the catalytic core of murine terminal deoxynucleotidyl transferase

1JMS · Terminal deoxynucleotidyltransferase: “Crystal structure of the catalytic core of murine terminal deoxynucleotidyl transferase”. X-ray diffraction, 2 ligands (MG, NA), 2 pockets (best druggability 0.68). MolNFT v1 #11440 on…

PDB: 1JMS
Type: protein
Length: 360 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Terminal deoxynucleotidyltransferase
EC: 2.7.7.31
UniProt: P09838
Ligands: MG, NA
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Terminal deoxynucleotidyltransferase (EC 2.7.7.31)	protein	360	49% helix, 14% strand	P09838

Ligands and binding sites

MG · Magnesium ion · metal · chains A
NA · Sodium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	810	0.68	0.75	68	MG, NA
2	72	0.38	0.78	16	empty

Compared structures

1JMS · Crystal Structure of the Catalytic Core of Murine Terminal Deoxynucleotidyl Transferase · the same entry in another collection · chain A against A, TM-score 1.00
P09838 · AlphaFold monomer V2.0 prediction for DNA nucleotidylexotransferase (P09838) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P09838
Elsewhere: RCSB PDB 1JMS · PDBe 1JMS · UniProt P09838

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