Structure of PDB 6mw3 Chain D

Receptor sequence
>6mw3D (length=673) Species: 1423 (Bacillus subtilis) [Search protein sequence]
NQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKE
KLDYLVENQYYEEEFLSLYSFEDIKEVFKTAYAKKFRFPSFMSAFKFYND
YALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPST
PTFLNAGRKELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKL
RAKGEAIKDVENATKGVVGVMKLLDNAFRYASGAAYLNIFHRDINDFLDT
KKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHM
DEMDMNEMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNV
NKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEEDEIGLDISCNLGSL
NILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLG
AMNLHGYLAQNGIAYESPEARDFANTFFMMVNFYSIQRSAEIAKEKGETF
DQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKKLKAF
VAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYP
MPGLASNNWFFYKEAYDMDMFKVVDMIATIQQHIDQGISFTLFLKDTMTT
RDLNRIDLYAHHRGIKTIYYART
3D structure
PDB6mw3 Convergent allostery in ribonucleotide reductase.
ChainD
Resolution4.65 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 peptide D T663 T664 R665 T649 T650 R651
BS02 DTP D K194 Y236 K188 Y230
BS03 DTP D D177 S178 L179 R207 I213 K214 D171 S172 L173 R201 I207 K208
BS04 DTP D F37 R90 F91 F34 R87 F88
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:6mw3, PDBe:6mw3, PDBj:6mw3
PDBsum6mw3
PubMed31201319
UniProtP50620|RIR1_BACSU Ribonucleoside-diphosphate reductase subunit alpha (Gene Name=nrdE)

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