Structure of PDB 6mve Chain A

Receptor sequence
>6mveA (length=680) Species: 1423 (Bacillus subtilis) [Search protein sequence]
VPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKL
DYLVENQYYEEEFLSLYSFEDIKEVFKTAYAKKFRFPSFMSAFKFYNDYA
LKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPT
FLNAGRKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSK
LRAKGEAIKDVENATKGVVGVMKLLDNAFRYADSGAAYLNIFHRDINDFL
DTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQ
HMDEMDMNEMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQD
NVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEEDEIGLDISCNLG
SLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIG
LGAMNLHGYLAQNGIAYESPEARDFANTFFMMVNFYSIQRSAEIAKEKGE
TFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKKLK
AFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTY
YPMPGLASNNWFFYKEAYDMDMFKVVDMIATIQQHIDQGISFTLFLKDTM
TTRDLNRIDLYAHHRGIKTIYYASCLSCVV
3D structure
PDB6mve Convergent allostery in ribonucleotide reductase.
ChainA
Resolution2.55 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 D177 S178 L179 R207 I213 K214 T220 D172 S173 L174 R202 I208 K209 T215
BS02 ADP A H34 F37 N42 R90 F91 R117 H29 F32 N37 R85 F86 R112
BS03 ATP A F47 F48 N50 L51 K54 Y85 F42 F43 N45 L46 K49 Y80
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:6mve, PDBe:6mve, PDBj:6mve
PDBsum6mve
PubMed31201319
UniProtP50620|RIR1_BACSU Ribonucleoside-diphosphate reductase subunit alpha (Gene Name=nrdE)

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