Structure of PDB 2alx Chain A

Receptor sequence
>2alxA (length=339) Species: 562 (Escherichia coli) [Search protein sequence]
AYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRP
EEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLIS
IPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRA
EGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSV
NALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLN
LLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLN
KDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWL
3D structure
PDB2alx Structure of Escherichia coli ribonucleotide reductase R2 in space group P6122.
ChainA
Resolution2.6 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 MN A D84 E115 H118 E238 D84 E115 H118 E238
BS02 MN A E115 E204 E238 H241 E115 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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2alx, PDBe:2alx, PDBj:2alx
PDBsum2alx
PubMed16301799
UniProtP69924|RIR2_ECOLI Ribonucleoside-diphosphate reductase 1 subunit beta (Gene Name=nrdB)

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