4P16: ORF1a

Crystal structure of the papain-like protease of Middle-East Respiratory Syndrome coronavirus. Determined by X-ray diffraction at 2.5 Å resolution. Released 7 May 2014.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Human betacoronavirus 2c EMC/2012
Chains: 1
Atoms: 2,508
Mol. weight: 36.31 kDa
Ligands: ZN
Released: 7 May 2014

Explore 4P16 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4P16 contains 13 α-helices and 19 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: 13 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	1
β-strand	16-21	6	1
α-helix	26-29	4
β-strand	33-35	3	1
β-strand	38-39	2	1
α-helix	44-45	2
α-helix	47-49	3
β-strand	53-56	4	1
α-helix	62-71	10
α-helix	79-90	12
β-strand	95-98	4	2
β-strand	101-104	4	2
α-helix	111-120	10
β-strand	126-128	3	3
α-helix	131-141	11
α-helix	146-156	11
α-helix	158-159	2
α-helix	166-174	9
β-strand	177-179	3	3
β-strand	184-191	8	4
β-strand	195-202	8	4
α-helix	203-207	5
β-strand	208-210	3	4
α-helix	215-219	5
α-helix	221	1
β-strand	222-225	4	4
β-strand	231-256	26	4
β-strand	265-269	5	4
β-strand	279-285	7	4
β-strand	288-292	5	4
β-strand	297-300	4	4
β-strand	302-318	17	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ORF1a	A	protein	326	Human betacoronavirus 2c EMC/2012	K0BWD0 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4P16_1 ORF1a (chains A)
GSHMASQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGADISDTIPDEKQNGHSL
YLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHGWKMVVCDKVRSLKLSDNNCYLN
AVIMTLDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVL
AKAELCCSARMVWREWCNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHR
QLVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHYVHARLKGGLILKFDS
GTVSKTSDWKCKVTDVLFPGQKYSSD

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Primary citation

Crystal structure of the papain-like protease of MERS coronavirus reveals unusual, potentially druggable active-site features. Lei, J., Mesters, J.R., Drosten, C. et al. Antiviral Res (2014) 109C:72-82. DOI 10.1016/j.antiviral.2014.06.011 · PubMed

Other PDB entries of the same protein (UniProt K0BWD0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5YNM 1.68 Å, Crystal structure of MERS-CoV nsp16/nsp10 complex bound to SAM and m7GpppA
5YNF 1.79 Å, Crystal structure of MERS-CoV nsp16/nsp10 complex bound to m7GpppA
5YNN 1.86 Å, Crystal structure of MERS-CoV nsp16/nsp10complex bound to sinefungin and m7GpppG
5YN6 1.95 Å, Crystal structure of MERS-CoV nsp10/nsp16 complex bound to SAM
5YNQ 1.96 Å, Crystal structure of MERS-CoV nsp16/nsp10 complex bound to SAH and m7GpppG
5YN5 1.96 Å, Crystal structure of MERS-CoV nsp10/nsp16 complex
5YNO 1.96 Å, Crystal structure of MERS-CoV nsp16/nsp10 complex bound to SAH and m7GpppA
5YN8 1.97 Å, Crystal structure of MERS-CoV nsp16/nsp10 complex bound to SAH
5YNB 1.98 Å, Crystal structure of MERS-CoV nsp16/nsp10 complex bound to Sinefungin
5YNJ 2.04 Å, Crystal structure of MERS-CoV nsp16/nsp10 complex bound to m7GpppG
5YNI 2.07 Å, Crystal structure of MERS-CoV nsp16/nsp10 complex bound to SAM and m7GpppG
5YNP 2.27 Å, Crystal structure of MERS-CoV nsp16/nsp10 complex bound to sinefungin and m7GpppA

Browse structure collections

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