Structure of PDB 4lil Chain A Binding Site BS02
Receptor Information
>4lil Chain A (length=370) Species:
9606
(Homo sapiens) [
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PTELPELLKLYYRRLFPYSQYYRWLNYIKNYFQHREFSFTLKDDIYIRYQ
SFNNQSDLEKEMQKMNPYKIDIGAVYSHRPNQHNTVKLGAFQAQEKELVF
DIDMTDYDDVRRCCSDICPKCWTLMTMAIRIIDRALKEDFGFKHRLWVYS
GRRGVHCWVCDESVRKLSSAVRSGIVEYLSLVKKKKVHLSEKIHPFIRKS
INIIKKYFEEYALVNQDILENKESWDKILALVPETIHDELQQSFQKSHNS
LQRWEHLKKVASRYQNNIKNDKYGPWLEWEIMLQYCFPRLDINVSKGINH
LLKSPFSVHPKTGRISVPIDLQKVDQFDPFTVPTISFICRELDATRDYKK
TSLAPYVKVFEHFLENLDKS
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
4lil Chain A Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
4lil
Insights into Eukaryotic Primer Synthesis from Structures of the p48 Subunit of Human DNA Primase.
Resolution
2.6 Å
Binding residue
(original residue number in PDB)
D109 H166
Binding residue
(residue number reindexed from 1)
D101 H156
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:4lil
,
PDBe:4lil
,
PDBj:4lil
PDBsum
4lil
PubMed
24239947
UniProt
P49642
|PRI1_HUMAN DNA primase small subunit (Gene Name=PRIM1)
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