Structure of PDB 5ci3 Chain A

Receptor sequence
>5ci3A (length=349) Species: 83334 (Escherichia coli O157:H7) [Search protein sequence]
AYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRP
EEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLIS
IPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRA
EGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSV
NALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLN
LLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLN
KDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQ
3D structure
PDB5ci3 Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example.
ChainA
Resolution2.401 Å
3D
structure
Catalytic site residues are labeled in the structure
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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:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0009263 deoxyribonucleotide biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5ci3, PDBe:5ci3, PDBj:5ci3
PDBsum5ci3
PubMed27276098
UniProtP69925|RIR2_ECO57 Ribonucleoside-diphosphate reductase 1 subunit beta (Gene Name=nrdB)

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