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Structure of a putative phosphomethylpyrimidine kinase from Acinetobacter baumannii

Analyse Structure of a putative phosphomethylpyrimidine kinase from Acinetobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4YL5
Type: protein
Length: 227 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.7
Source: Acinetobacter baumannii IS-123
Molecule: Putative phosphomethylpyrimidine kinase
UniProt: J5A2R3
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · resolution 1.7 · 1 distinct chain · 37% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative phosphomethylpyrimidine kinase	protein	227	37% helix, 27% strand	J5A2R3

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 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	211	0.60	0.81	37	EDO

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4YL5 · Structure of a putative phosphomethylpyrimidine kinase from acinetobacter baumannii · 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 J5A2R3
Elsewhere: RCSB PDB 4YL5 · PDBe 4YL5 · UniProt J5A2R3

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