Structure of PDB 6nfe Chain B

Receptor sequence

>6nfeB (length=299) Species: 446 (Legionella pneumophila)

STMMIFTGNANPELALKISSHLQIPIGKATVGTFSDGETMVEILENVRGK
DVFVLQSTCAPANNNLMELLIMADALRRSSAGRITAVVPYFGYARQDRRV
RSARVPITAKVVADMMASVGICRVLTVDLHADQIQGFFYMPVDNVYSTPV
LLEDITKQKLNNIMIVSPDVGGVVRARAVAKRLNDAELSIIDKRRSEVMH
IIGEPANKNCIIVDDIVDTAGTLCTAAHELKKNGAKSVRAYITHPVLSGP
AVNNIKHSGLDEVVVTDTIPLSAEAQNCEKIRVVSLADMLAQAIKRVNV

3D structure

• PDB: 6nfe Crystal Structure of Ribose-phosphate Pyrophosphokinase from Legionella pneumophila with bound AMP, ADP, and Ribose-5-Phosphate
• Chain: B
• Resolution: 1.75 Å

Enzymatic activity

• Enzyme Commision number: 2.7.6.1: ribose-phosphate diphosphokinase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ADP	B	R96 Q97 H131	R95 Q96 H130
BS02	ADP	B	F35 D37 E39	F34 D36 E38
BS03	HSX	B	H131 D220 D221 I222 D224 T225 A226 T228	H130 D214 D215 I216 D218 T219 A220 T222

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004749 ribose phosphate diphosphokinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006015 5-phosphoribose 1-diphosphate biosynthetic process
• GO:0006164 purine nucleotide biosynthetic process
• GO:0009156 ribonucleoside monophosphate biosynthetic process
• GO:0009165 nucleotide biosynthetic process
• GO:0016310 phosphorylation
• GO:0044249 cellular biosynthetic process

Cellular Component

• GO:0002189 ribose phosphate diphosphokinase complex
• GO:0005737 cytoplasm

External links

• PDB: RCSB:6nfe, PDBe:6nfe, PDBj:6nfe
• PDBsum: 6nfe
• UniProt: Q5ZY30