Structure of PDB 5ci2 Chain A

Receptor sequence

>5ci2A (length=349) Species: 83334 (Escherichia coli O157:H7)

AYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRP
EEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLIS
IPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRA
EGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSV
NALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLN
LLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLN
KDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQ

3D structure

• PDB: 5ci2 Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example.
• Chain: A
• Resolution: 2.25 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y122 D237
• Catalytic site (residue number reindexed from 1): Y122 D237
• Enzyme Commision number: 1.17.4.1: ribonucleoside-diphosphate reductase.

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	FEO	A	D84 E115 H118 E204 E238 H241	D84 E115 H118 E204 E238 H241

Gene Ontology

Molecular Function

• GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
• GO:0005506 iron ion binding
• GO:0005515 protein binding
• GO:0016491 oxidoreductase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0009185 ribonucleoside diphosphate metabolic process
• GO:0009263 deoxyribonucleotide biosynthetic process
• GO:0009265 2'-deoxyribonucleotide biosynthetic process
• GO:0015949 nucleobase-containing small molecule interconversion

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0005971 ribonucleoside-diphosphate reductase complex

External links

• PDB: RCSB:5ci2, PDBe:5ci2, PDBj:5ci2
• PDBsum: 5ci2
• PubMed: 27276098
• UniProt: P69924|RIR2_ECOLI Ribonucleoside-diphosphate reductase 1 subunit beta (Gene Name=nrdB)