Structure of PDB 1peq Chain A

Receptor sequence
>1peqA (length=679) [Search protein sequence]
RVMQETMDYHALNAMLNLYDKAGHIQFDKDQQAIDAFFATHVRPHSVTFA
SQHERLGTLVREGYYDDAVLARYDRAFVLRLFEHAHASGFRFQTFLGAWK
FYTSYTLKTFDGKRYLEHFEDRVTMVALTLAQGDETLATQLTDEMLSGRF
QPATPTFLNCGKQQRGELVSCFLLRIEDNMESIGRAVNSALQLSKRGGGV
AFLLSNLREAGAPIKRIENQSSGVIPVMKMLEDAFSYANQGAGAVYLHAH
HPDILRFLDTKRIKTLSLGVVIPDITFRLAKENAQMALFSPYDIQRRYGK
PFGDIAISERYDELIADPHVRKTYINARDFFQTLAEIQFESGYPYIMFED
TVNRANPIAGRINMSNLCSEILQVNSASRYDDNLDYTHIGHDISCNLGSL
NIAHVMDSPDIGRTVETAIRGLTAVSDMSHIRSVPSIAAGNAASHAIGLG
QMNLHGYLAREGIAYGSPEALDFTNLYFYTITWHAVHTSMRLARERGKTF
AGFAQSRYASGDYFTQYLQDDWQPKTAKVRALFARSGITLPTREMWLKLR
DDVMRYGIYNQNLQAVPPTGSISYINHATSSIHPIVAKIEIRKEGKTGRV
YYPAPFMTNENLDMYQDAYDIGPEKIIDTYAEATRHVDQGLSLTLFFPDT
ATTRDINKAQIYAWRKGIKSLYYIRLRQL
3D structure
PDB1peq Structure of the large subunit of class Ib ribonucleotide reductase from Salmonella typhimurium and its complexes with allosteric effectors.
ChainA
Resolution2.8 Å
3D
structure
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Enzymatic activity
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 TTP A D185 N186 M187 R215 I221 K222 S228 D178 N179 M180 R208 I214 K215 S221
Gene Ontology
Molecular Function
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO:0005524 ATP binding
GO:0016491 oxidoreductase activity
Biological Process
GO:0009263 deoxyribonucleotide biosynthetic process
Cellular Component
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:1peq, PDBe:1peq, PDBj:1peq
PDBsum1peq
PubMed12818204
UniProtQ08698|RIR3_SALTY Ribonucleoside-diphosphate reductase 2 subunit alpha (Gene Name=nrdE)

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