4C2X: Human N-myristoyltransferase isoform 2

Name: PDB 4C2X: Human N-myristoyltransferase isoform 2 (NMT2)
Published: 2014-10-01
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Human N-myristoyltransferase isoform 2 (NMT2). Determined by X-ray diffraction at 2.33 Å resolution. Released 1 Oct 2014.

Method: X-ray diffraction
Resolution: 2.33 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 3,345
Mol. weight: 48.61 kDa
Ligands: NHW, MG
Released: 1 Oct 2014

Explore 4C2X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4C2X contains 17 α-helices and 22 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 17 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	120-122	3
α-helix	126-127	2
β-strand	136	1	1
α-helix	149-153	5
β-strand	156-160	5	2
α-helix	166-179	14
β-strand	182	1	3
β-strand	188-190	3	3
α-helix	194-201	8
α-helix	208-210	3
β-strand	211-216	6	2
β-strand	222-235	14	2
β-strand	238-250	13	2
α-helix	252-254	3
α-helix	260-272	13
β-strand	279-283	5	2
β-strand	292-300	9	2
α-helix	303-308	6
α-helix	320-326	7
β-strand	338-340	3	2
α-helix	343-345	3
α-helix	346-356	11
α-helix	357-359	3
β-strand	362-364	3	2
α-helix	368-375	8
β-strand	378	1	2
β-strand	382-388	7	2
β-strand	394-402	9	2
β-strand	405-407	3	3
β-strand	415-416	2	3
β-strand	418-421	4	2
β-strand	425-426	2	2
α-helix	431-443	13
β-strand	449-453	5	2
α-helix	458-460	3
β-strand	468-479	12	2
β-strand	482	1	1
α-helix	488-490	3
β-strand	491	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glycylpeptide N-tetradecanoyltransferase 2	A	protein	410	HOMO SAPIENS	O60551 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4C2X_1 GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE 2 (chains A)
MGSSHHHHHHSSGLEVLFQGPHMDEAAKHRYQFWDTQPVPKLDEVITSHGAIEPDKDNVR
QEPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGW
LLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHKKLRSKRVAPVLIRE
ITRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPKKLVEVKFSHLSRNMTLQRTMKL
YRLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEVAHWFLPREHIIDTFV
VESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMSDALILAKSKG
FDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVGLVLQ

Ligands and cofactors

ID	Name	Formula	Copies
NHW	2-oxopentadecyl-CoA	C36 H64 N7 O17 P3 S	1
MG	Magnesium ion	Mg	1

Primary citation

Global Profiling of Co- and Post-Translationally N-Myristoylated Proteomes in Human Cells. Thinon, E., Serwa, R.A., Broncel, M. et al. Nat Commun (2014) 5:4919. DOI 10.1038/NCOMMS5919 · PubMed

Other PDB entries of the same protein (UniProt O60551 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6PAU 1.93 Å, Structure of Human NMT2 with myristoyl-lysine peptide and CoA products
9NDP 2.82 Å, Structure of stalled ribosome and nascent chain in complex with NMT2 and NAC

Browse structure collections

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