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Crystal structure of fructokinase from brucella abortus 2308 with bound amppnp

Analyse Crystal structure of fructokinase from brucella abortus 2308 with bound amppnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WJM
Type: protein
Length: 312 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RIBOKINASE:CARBOHYDRATE kinase, pfkb
EC: 2.7.1.4
UniProt: Q2YNY7
Ligands: ANP, MG
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RIBOKINASE:CARBOHYDRATE kinase, pfkb (EC 2.7.1.4)	protein	312	37% helix, 22% strand	Q2YNY7

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
MG · Magnesium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A
MLA · Malonic acid · additive · 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	593	0.71	0.79	64	ANP, MG
2	67	0.31	0.75	19	empty

Compared structures

4WJM · Crystal structure of Fructokinase from Brucella abortus 2308 with bound AMPPNP · 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 Q2YNY7
Elsewhere: RCSB PDB 4WJM · PDBe 4WJM · UniProt Q2YNY7

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