Structure of PDB 3n37 Chain A

Receptor sequence
>3n37A (length=284) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
RISAINWNKISDDKDLEVWNRLTSNFWLPEKVPLSNDIPAWQTLTVVEQQ
LTMRVFTGLTLLDTLQNVIGAPSLMPDALTPHEEAVLSNISFMEAVHARS
YSSIFSTLCQTKDVDAAYAWSEENAPLQRKAQIIQQHYRGDDPLKKKIAS
VFLESFLFYSGFWLPMYFSSRGKLTNTADLIRLIIRDEAVHGYYIGYKYQ
KNMEKISLGQREELKSFAFDLLLELYDNELQYTDELYAETPWADDVKAFL
CYNANKALMNLGYEPLFPAEMAEVNPAILAALSP
3D structure
PDB3n37 Structural basis for activation of class Ib ribonucleotide reductase.
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y105 D191
Catalytic site (residue number reindexed from 1) Y101 D187
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 D67 E98 H101 E158 E192 D63 E94 H97 E154 E188
BS02 MN A E98 E158 E192 H195 E94 E154 E188 H191
Gene Ontology
Molecular Function
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0030145 manganese ion 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
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:3n37, PDBe:3n37, PDBj:3n37
PDBsum3n37
PubMed20688982
UniProtP37146|RIR4_ECOLI Ribonucleoside-diphosphate reductase 2 subunit beta (Gene Name=nrdF)

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