Structure of PDB 4erp Chain F

Receptor sequence

>4erpF (length=358) Species: 83333 (Escherichia coli K-12)

AYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRP
EEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLIS
IPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRA
EGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSV
NALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLN
LLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLN
KDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQSEVDT
DDLSNFQL

3D structure

• PDB: 4erp Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase.
• Chain: F
• Resolution: 4.45 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	F	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:4erp, PDBe:4erp, PDBj:4erp
• PDBsum: 4erp
• PubMed: 22727814
• UniProt: P69924|RIR2_ECOLI Ribonucleoside-diphosphate reductase 1 subunit beta (Gene Name=nrdB)