Structure of PDB 6r4t Chain A Binding Site BS01
Receptor Information
>6r4t Chain A (length=384) Species:
9606
(Homo sapiens) [
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PTELPELLKLYYRRLFPYSQYYRWLNYGGVIKNYFQHREFSFTLKDDIYI
RYQSFNNQSDLEKEMQKMNPYKIDIGAVYSHRPNQHNTVKLGAFQAQEKE
LVFDIDMTDYDDVRRCCSSADICPKCWTLMTMAIRIIDRALKEDFGFKHR
LWVYSGRRGVHCWVCDESVRKLSSAVRSGIVEYLSLVKGGQDVKKKVHLS
EKIHPFIRKSINIIKKYFEEYALVNQDILENKESWDKILALVPETIHDEL
QQSFQKSHNSLQRWEHLKKVASRYQNNIKNDKYGPWLEWEIMLQYCFPRL
DINVSKGINHLLKSPFSVHPKTGRISVPIDLQKVDQFDPFTVPTISFICR
ELDAISTRDYKKTSLAPYVKVFEHFLENLDKSRK
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
6r4t Chain A Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
6r4t
Structural Basis for Inhibition of Human Primase by Arabinofuranosyl Nucleoside Analogues Fludarabine and Vidarabine.
Resolution
2.35 Å
Binding residue
(original residue number in PDB)
C121 C122 C128 C131
Binding residue
(residue number reindexed from 1)
C116 C117 C123 C126
Annotation score
1
Enzymatic activity
Enzyme Commision number
2.7.7.102
: DNA primase AEP.
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
PDBsum
6r4t
PubMed
31479243
UniProt
P49642
|PRI1_HUMAN DNA primase small subunit (Gene Name=PRIM1)
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