MolNFT v2 · #211734 · protein

Crystal structure of chemically modified E. coli ThrS catalytic domain 3

8H9B · Threonine--tRNA ligase: “Crystal structure of chemically modified E. coli ThrS catalytic domain 3”. X-ray diffraction at 2.23, 2 ligands (X5V, ZN), 2 pockets (best druggability 0.65). MolNFT v2 #211734 on GenesisL1: 3D structure…

PDB: 8H9B
Type: protein
Length: 399 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.23
Source: Escherichia coli
Molecule: Threonine--tRNA ligase
EC: 6.1.1.3
UniProt: E2QMS9
Ligands: X5V, ZN
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · resolution 2.23 · 1 distinct chain · 39% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Threonine--tRNA ligase (EC 6.1.1.3)	protein	399	39% helix, 27% strand	E2QMS9

Ligands and binding sites

X5V · N-(2,3-dihydroxybenzoyl)-4-(4-nitrophenyl)-L-threonine · ligand · chains A
ZN · Zinc 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	494	0.65	0.77	36	X5V, ZN
2	83	0.42	0.78	19	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

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 E2QMS9
Elsewhere: RCSB PDB 8H9B · PDBe 8H9B · UniProt E2QMS9

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