4N49: Cap-specific mRNA-methyltransferase 1

Name: PDB 4N49: Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 Protein in complex with m7GpppG and SAM
Published: 2014-01-22
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 Protein in complex with m7GpppG and SAM. Determined by X-ray diffraction at 1.9 Å resolution. Released 22 Jan 2014.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,877
Mol. weight: 49.9 kDa
Ligands: MGT, SAM
Released: 22 Jan 2014

Explore 4N49 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4N49 contains 22 α-helices and 12 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: 22 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	146-149	4
β-strand	157	1	1
α-helix	158-161	4
α-helix	164-167	4
β-strand	176-179	4	2
α-helix	193-204	12
α-helix	205-208	4
α-helix	211-221	11
α-helix	225-227	3
α-helix	235-246	12
β-strand	255	1	3
β-strand	261	1	3
α-helix	265-267	3
α-helix	269-270	2
β-strand	271-276	6	1
α-helix	282-291	10
β-strand	295-300	6	1
α-helix	310-312	3
β-strand	322-323	2	1
α-helix	339-351	13
β-strand	358-363	6	1
α-helix	373-375	3
α-helix	376-379	4
α-helix	381-394	14
β-strand	395-405	11	1
α-helix	411-423	13
β-strand	424-430	7	1
β-strand	442-449	8	1
α-helix	450	1
α-helix	454-470	17
β-strand	475-479	5	2
α-helix	483-487	5
α-helix	490-519	30
α-helix	528-539	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1	A	protein	428	Homo sapiens	Q8N1G2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4N49_1 Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (chains A)
GAMRGLGLTLRGFDQELNVDWRDEPEPSACEQVSWFPECTTEIPDTQEMSDWMVVGKRKM
IIEDETEFCGEELLHSVLQCKSVFDVLDGEEMRRARTRANPYEMIRGVFFLNRAAMKMAN
MDFVFDRMFTNPRDSYGKPLVKDREAELLYFADVCAGPGGFSEYVLWRKKWHAKGFGMTL
KGPNDFKLEDFYSASSELFEPYYGEGGIDGDGDITRPENISAFRNFVLDNTDRKGVHFLM
ADGGFSVEGQENLQEILSKQLLLCQFLMALSIVRTGGHFICKTFDLFTPFSVGLVYLLYC
CFERVCLFKPITSRPANSERYVVCKGLKVGIDDVRDYLFAVNIKLNQLRNTDSDVNLVVP
LEVIKGDHEFTDYMIRSNESHCSLQIKALAKIHAFVQDTTLSEPRQAEIRKECLRLWGIP
DQARVAPS

Ligands and cofactors

ID	Name	Formula	Copies
MGT	7N-methyl-8-hydroguanosine-5'-triphosphate	C11 H20 N5 O14 P3	1
SAM	S-adenosylmethionine	C15 H22 N6 O5 S	1

Water and common crystallization additives (NA) are not listed.

Primary citation

Structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation. Smietanski, M., Werner, M., Purta, E. et al. Nat Commun (2014) 5:3004-3004. DOI 10.1038/ncomms4004 · PubMed

Other PDB entries of the same protein (UniProt Q8N1G2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4N4A 2.35 Å, Cystal structure of Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1
4N48 2.7 Å, Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 Protein in complex with capped…
8P4E 3.9 Å, Structural insights into human co-transcriptional capping - structure 5
8P4F 4.0 Å, Structural insights into human co-transcriptional capping - structure 6
8W8F 4.0 Å, human co-transcriptional RNA capping enzyme RNGTT-CMTR1

Browse structure collections

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