Structure of PDB 6r4t Chain A

Receptor sequence
>6r4tA (length=384) Species: 9606 (Homo sapiens) [Search protein sequence]
PTELPELLKLYYRRLFPYSQYYRWLNYGGVIKNYFQHREFSFTLKDDIYI
RYQSFNNQSDLEKEMQKMNPYKIDIGAVYSHRPNQHNTVKLGAFQAQEKE
LVFDIDMTDYDDVRRCCSSADICPKCWTLMTMAIRIIDRALKEDFGFKHR
LWVYSGRRGVHCWVCDESVRKLSSAVRSGIVEYLSLVKGGQDVKKKVHLS
EKIHPFIRKSINIIKKYFEEYALVNQDILENKESWDKILALVPETIHDEL
QQSFQKSHNSLQRWEHLKKVASRYQNNIKNDKYGPWLEWEIMLQYCFPRL
DINVSKGINHLLKSPFSVHPKTGRISVPIDLQKVDQFDPFTVPTISFICR
ELDAISTRDYKKTSLAPYVKVFEHFLENLDKSRK
3D structure
PDB6r4t Structural Basis for Inhibition of Human Primase by Arabinofuranosyl Nucleoside Analogues Fludarabine and Vidarabine.
ChainA
Resolution2.35 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.102: DNA primase AEP.
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 ZN A C121 C122 C128 C131 C116 C117 C123 C126
BS02 MN A D109 D111 H166 D104 D106 H161
BS03 HEJ A K77 D79 D109 D111 S160 R162 R163 H166 L316 L317 K318 H324 K72 D74 D104 D106 S155 R157 R158 H161 L311 L312 K313 H319
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003896 DNA primase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016779 nucleotidyltransferase activity
GO:0032553 ribonucleotide binding
GO:0046872 metal ion binding
Biological Process
GO:0006260 DNA replication
GO:0006269 DNA replication, synthesis of primer
GO:0006270 DNA replication initiation
Cellular Component
GO:0000428 DNA-directed RNA polymerase complex
GO:0005654 nucleoplasm
GO:0005658 alpha DNA polymerase:primase complex
GO:0016020 membrane
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:6r4t, PDBe:6r4t, PDBj:6r4t
PDBsum6r4t
PubMed31479243
UniProtP49642|PRI1_HUMAN DNA primase small subunit (Gene Name=PRIM1)

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