Structure of PDB 6t66 Chain C

Receptor sequence
>6t66C (length=440) Species: 666 (Vibrio cholerae) [Search protein sequence]
KVPPHSLEAEQSVIGGLLLDNERWDTVSEHVMTQDFYSRPHRLIFDGVKS
ILEAGKPLDLITLSEYLEQREQLEDVGGFAYLADLAKNTPSAANINAYAE
IVAERALVRNLIGVANEIADAGYDPQGRNAEDLLDLAESKVFAIAEARTS
ENEGPKNVDSILERTLERIELLYKTPQDGVTGVNTGFTDLNKKTAGLQGS
DLIIVAARPSMGKTTFAMNLCENAAMEQDKPVLIFSLEMPAEQIMMRMLA
SLSRVDQTKIRTGQLDDEDWARISSTMGILMEKKNMYIDDSSGLTPTEVR
SRARRIAREHGGLSLIMVDYLQLMRVPALTDNRTLEIAEISRSLKALAKE
LNVPVVALSQLNRSLEQRADKRPVNSDLRESGSIEQDADLIMFIYRDEVY
HPDSPLKGTAEIIIGKQRNGPIGSVRLTFQGHYSRFDNYA
3D structure
PDB6t66 Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase.
ChainC
Resolution3.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.4.12: DNA helicase.
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 GDP C Q438 R439 N440 G441 Q417 R418 N419 G420
BS02 ALF C K437 R439 K416 R418
BS03 GDP C S231 G233 K234 T235 T236 R268 Q278 G452 S210 G212 K213 T214 T215 R247 Q257 G431
BS04 ALF C K234 E259 Y341 K213 E238 Y320
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003678 DNA helicase activity
GO:0004386 helicase activity
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0046872 metal ion binding
Biological Process
GO:0006260 DNA replication
GO:0006268 DNA unwinding involved in DNA replication
GO:0006269 DNA replication, synthesis of primer
Cellular Component
GO:0005829 cytosol
GO:1990077 primosome complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6t66, PDBe:6t66, PDBj:6t66
PDBsum6t66
PubMed34107018
UniProtQ9KUY7

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