Structure of PDB 5exr Chain F

Receptor sequence
>5exrF (length=434) Species: 9606 (Homo sapiens) [Search protein sequence]
YPHCLQFYLQPPSENISLIEFENLAIDRVKLLKSVENLGVSYVKGTEQYQ
SKLESELRKLKFSYRENLEDEYEPRRRDHISHFILRLAYCQSEELRRWFI
QQEMDLLRFRFSILPKDKIQDFLKDSQLQFEAISDEEKTLREQEIVASSP
SLSGLKLGFESIYKIPFADALDLFRGRKVYLEDGFAYVPLKDIVAIILNE
FRAKLSKALALTARSLPAVQSDERLQPLLNHLSHSYTGQDYSTQGNVGKI
SLDQIDLLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGLFLKGIGLTLE
QALQFWKQEFIKGKMDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCLKII
LSNPPSQGDYHGCPFRHSDPELLKQKLQSYKISPGGISQILDLVKGTHYQ
VACQKYFEMIHNVDDCGFSLNHPNQFFCESQRIL
3D structure
PDB5exr Mechanism of Concerted RNA-DNA Primer Synthesis by the Human Primosome.
ChainF
Resolution3.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.-
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 SF4 F P285 C287 C367 C384 Q421 C424 P444 P264 C266 C346 C363 Q400 C403 P423
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0005515 protein binding
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
GO:0071667 DNA/RNA hybrid binding
Biological Process
GO:0006260 DNA replication
GO:0006261 DNA-templated DNA replication
GO:0006269 DNA replication, synthesis of primer
GO:0006270 DNA replication initiation
GO:1903934 positive regulation of DNA primase activity
Cellular Component
GO:0005654 nucleoplasm
GO:0005658 alpha DNA polymerase:primase complex
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:5exr, PDBe:5exr, PDBj:5exr
PDBsum5exr
PubMed26975377
UniProtP49643|PRI2_HUMAN DNA primase large subunit (Gene Name=PRIM2)

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