MolNFT v1 · #17063 · protein

Acetylglutamate kinase from escherichia COLI complexed with ADP and sulphate

1OHB: “Acetylglutamate kinase from escherichia COLI complexed with ADP and sulphate”. X-ray diffraction, 2 ligands (ADP, SO4), 3 pockets (best druggability 0.67). MolNFT v1 #17063 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1OHB
Type: protein
Length: 258 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetylglutamate kinase
EC: 2.7.2.8
UniProt: P11445
Ligands: ADP, SO4
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetylglutamate kinase (EC 2.7.2.8)	protein	258	41% helix, 24% strand	P11445

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
SO4 · Sulfate ion · ion · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

3 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	390	0.67	0.80	42	SO4, ADP, ACT
2	65	0.32	0.76	16	empty
3	57	0.32	0.77	13	empty

Compared structures

1OHB · Acetylglutamate kinase from Escherichia coli complexed with ADP and sulphate · 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 P11445
Elsewhere: RCSB PDB 1OHB · PDBe 1OHB · UniProt P11445

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