4N48: Cap-specific mRNA-methyltransferase 1

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 Protein in complex with capped RNA fragment. Determined by X-ray diffraction at 2.7 Å resolution. Released 22 Jan 2014.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,807
Mol. weight: 102.23 kDa
Ligands: SAM, MGT
Released: 22 Jan 2014

Explore 4N48 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4N48 contains 48 α-helices and 23 β-strands across 2 chains. 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: 25 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	143-145	3
α-helix	147-149	3
β-strand	157	1	1
α-helix	158-161	4
α-helix	164-166	3
α-helix	170-173	4
β-strand	176-179	4	2
α-helix	180-181	2
α-helix	193-204	12
α-helix	205-208	4
α-helix	211-221	11
α-helix	225-227	3
α-helix	236-246	11
β-strand	255	1	3
β-strand	261	1	3
α-helix	270	1
β-strand	271-276	6	1
α-helix	282-291	10
β-strand	295-300	6	1
α-helix	310-312	3
β-strand	321-323	3	1
α-helix	329-331	3
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	483-486	4
α-helix	490-519	30
α-helix	528-539	12

Chain B: 23 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	147-149	3
α-helix	158-161	4
α-helix	164-166	3
α-helix	168-171	4
β-strand	176-179	4	4
α-helix	193-204	12
α-helix	205-207	3
α-helix	211-221	11
α-helix	225-227	3
α-helix	236-246	11
β-strand	255	1	5
β-strand	261	1	5
β-strand	271-276	6	6
α-helix	282-291	10
α-helix	292-294	3
β-strand	295-300	6	6
α-helix	310-312	3
β-strand	321-323	3	6
α-helix	329-331	3
α-helix	339-351	13
β-strand	358-363	6	6
α-helix	373-375	3
α-helix	376-379	4
α-helix	381-394	14
β-strand	395-405	11	6
α-helix	411-423	13
β-strand	424-430	7	6
β-strand	442-449	8	6
α-helix	450	1
α-helix	454-469	16
β-strand	475-479	5	4
α-helix	483-488	6
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, B	protein	428	Homo sapiens	Q8N1G2 (AlphaFold model)
capped RNA	D, G	RNA	4

Sequence of entity 1 (A, B), FASTA

>4N48_1 Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (chains A, B)
GAMRGLGLTLRGFDQELNVDWRDEPEPSACEQVSWFPECTTEIPDTQEMSDWMVVGKRKM
IIEDETEFCGEELLHSVLQCKSVFDVLDGEEMRRARTRANPYEMIRGVFFLNRAAMKMAN
MDFVFDRMFTNPRDSYGKPLVKDREAELLYFADVCAGPGGFSEYVLWRKKWHAKGFGMTL
KGPNDFKLEDFYSASSELFEPYYGEGGIDGDGDITRPENISAFRNFVLDNTDRKGVHFLM
ADGGFSVEGQENLQEILSKQLLLCQFLMALSIVRTGGHFICKTFDLFTPFSVGLVYLLYC
CFERVCLFKPITSRPANSERYVVCKGLKVGIDDVRDYLFAVNIKLNQLRNTDSDVNLVVP
LEVIKGDHEFTDYMIRSNESHCSLQIKALAKIHAFVQDTTLSEPRQAEIRKECLRLWGIP
DQARVAPS

Sequence of entity 2 (D, G), FASTA

>4N48_2 capped RNA (chains D, G)
GAUC

Ligands and cofactors

ID	Name	Formula	Copies
SAM	S-adenosylmethionine	C15 H22 N6 O5 S	2
MGT	7N-methyl-8-hydroguanosine-5'-triphosphate	C11 H20 N5 O14 P3	2

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:

4N49 1.9 Å, Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 Protein in complex with m7GpppG…
4N4A 2.35 Å, Cystal structure of Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1
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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