Structure of PDB 4c2z Chain A Binding Site BS03
Receptor Information
>4c2z Chain A (length=382) Species:
9606
(Homo sapiens) [
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RSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLG
DRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGV
RVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLI
REITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHL
SRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQFHLTP
VMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHK
SLKAAYSFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEK
LKFGIGDGNLQYYLYNWKCPSMGAEKVGLVLQ
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
4c2z Chain A Residue 1499 [
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Receptor-Ligand Complex Structure
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PDB
4c2z
Chemical Proteomics Defines the Mammalian N- Myristoylated Proteome in Live Cells Global Profiling of Co- and Post-Translationally N-Myristoylated Proteomes in Human Cells.
Resolution
2.08 Å
Binding residue
(original residue number in PDB)
L254 R255 S256 K257 V259
Binding residue
(residue number reindexed from 1)
L140 R141 S142 K143 V145
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
N246 F247 L248 T282 Q496
Catalytic site (residue number reindexed from 1)
N132 F133 L134 T168 Q382
Enzyme Commision number
2.3.1.-
2.3.1.97
: glycylpeptide N-tetradecanoyltransferase.
Gene Ontology
Molecular Function
GO:0004379
glycylpeptide N-tetradecanoyltransferase activity
Biological Process
GO:0006499
N-terminal protein myristoylation
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:4c2z
,
PDBe:4c2z
,
PDBj:4c2z
PDBsum
4c2z
PubMed
25255805
UniProt
P30419
|NMT1_HUMAN Glycylpeptide N-tetradecanoyltransferase 1 (Gene Name=NMT1)
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