MolNFT v1 · #111640 · protein

Structure of a putative phosphomethylpyrimidine kinase from acinetobacter baumannii in non-covalent complex with pyridoxal phosphate

4YWR · Putative hydroxymethylpyrimidine…: “Structure of a putative phosphomethylpyrimidine kinase from acinetobacter baumannii in non-covalent complex…”. X-ray diffraction, 1 ligand (PLP), 1 pocket (best druggability 0.61). MolNFT v1…

PDB: 4YWR
Type: protein
Length: 228 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative hydroxymethylpyrimidine KINASE/PHOSPHOMETHYLPYRIMIDINE kinase
UniProt: A0A0A2TKW6
Ligands: PLP
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative hydroxymethylpyrimidine KINASE/PHOSPHOMETHYLPYRIMIDINE kinase	protein	228	39% helix, 29% strand	A0A0A2TKW6

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · 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	240	0.61	0.81	43	PLP

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4YWR · Structure of a putative phosphomethylpyrimidine kinase from Acinetobacter baumannii in… · 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 A0A0A2TKW6
Elsewhere: RCSB PDB 4YWR · PDBe 4YWR · UniProt A0A0A2TKW6

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