5NXS: Human Pro-myostatin Precursor

Crystal Structure of Human Pro-myostatin Precursor at 4.2 A Resolution with Experimental Phases from SeMet labelling. Determined by X-ray diffraction at 4.19 Å resolution. Released 17 Jan 2018.

Method: X-ray diffraction
Resolution: 4.19 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,556
Mol. weight: 77 kDa
Released: 17 Jan 2018

Explore 5NXS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NXS contains 12 α-helices and 35 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: 6 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	44-63	20
α-helix	74-80	7
α-helix	85-91	7
β-strand	114-120	7	1
β-strand	122-123	2	2
β-strand	139-140	2	2
β-strand	151-160	10	1
α-helix	161-163	3
β-strand	169-175	7	3
β-strand	187-194	8	3
β-strand	202-207	6	1
α-helix	209-217	9
α-helix	219-221	3
β-strand	225-231	7	3
β-strand	236	1	3
β-strand	238	1	1
β-strand	252-257	6	1
β-strand	284	1	4
β-strand	287-289	3	5
β-strand	300	1	6
β-strand	303-305	3	5
β-strand	308	1	4
β-strand	340-353	14	6
β-strand	359-374	16	6

Chain B: 6 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	45-63	19
α-helix	74-80	7
α-helix	85-91	7
β-strand	115-120	6	6
β-strand	151-157	7	6
α-helix	159	1
β-strand	160	1	7
α-helix	161-163	3
β-strand	169-174	6	8
β-strand	189-194	6	8
β-strand	205-207	3	6
α-helix	209-217	9
β-strand	226-230	5	8
β-strand	236	1	8
β-strand	238	1	7
β-strand	252-257	6	6
β-strand	281-284	4	9
β-strand	287-289	3	10
β-strand	300	1	1
β-strand	303-305	3	10
β-strand	308-311	4	9
β-strand	340-352	13	1
β-strand	358-374	17	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Growth/differentiation factor 8	A, B	protein	335	Homo sapiens	O14793 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5NXS_1 Growth/differentiation factor 8 (chains A, B)
GSTWRQNTKSSRIEAIKIQILSKLRLETAPNISKDVIRQLLPKAPPLRELIDQYDVQRDD
SSDGSLEDDDYHATTETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYL
RPVETPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPE
SNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESR
CCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCC
TPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS

Primary citation

Structure of the human myostatin precursor and determinants of growth factor latency. Cotton, T.R., Fischer, G., Wang, X. et al. EMBO J (2018) 37:367-383. DOI 10.15252/embj.201797883 · PubMed

Other PDB entries of the same protein (UniProt O14793 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5F3B 1.76 Å, Structure of myostatin in complex with chimeric RK35 antibody
5NTU 2.58 Å, Crystal Structure of human Pro-myostatin Precursor at 2.6 A Resolution
5F3H 2.7 Å, Structure of myostatin in complex with humanized RK35 antibody
6UMX 2.79 Å, Structural basis for specific inhibition of extracellular activation of pro/latent…

Browse structure collections

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