1S01: Subtilisin BPN'

Large increases in general stability for subtilisin bpn(prime) through incremental changes in the free energy of unfolding. Determined by X-ray diffraction at 1.7 Å resolution. Released 15 Oct 1990.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Bacillus amyloliquefaciens
Chains: 1
Atoms: 2,162
Mol. weight: 27.7 kDa
Ligands: IPA, CA
Released: 15 Oct 1990

Explore 1S01 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1S01 contains 11 α-helices and 16 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: 11 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	6-10	5
α-helix	13-18	6
β-strand	27-32	6	1
β-strand	44-49	6	1
β-strand	51	1	2
β-strand	54	1	2
α-helix	64-73	10
β-strand	89-94	6	1
α-helix	104-116	13
β-strand	121-124	4	1
β-strand	128	1	3
α-helix	133-144	12
β-strand	148-152	5	1
β-strand	167	1	3
β-strand	175-180	6	1
α-helix	185	1
β-strand	186	1	1
α-helix	187	1
β-strand	198-201	4	1
β-strand	205-209	5	4
β-strand	213-217	5	4
α-helix	220-237	18
α-helix	243-252	10
β-strand	255	1	1
α-helix	260-263	4
β-strand	267	1	1
α-helix	270-273	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Subtilisin BPN'	A	protein	275	Bacillus amyloliquefaciens	P00782 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1S01_1 Subtilisin BPN' (chains A)
AQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASFVPSETNPFQD
NNSHGTHVAGTVAALDNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMD
VINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPAKYPSVIAVGAV
DSSNQRASFSSVGPELDVMAPGVSICSTLPGNKYGAKSGTSMASPHVAGAAALILSKHPN
WTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQ

Ligands and cofactors

ID	Name	Formula	Copies
IPA	Isopropyl alcohol	C3 H8 O	2
CA	Calcium ion	Ca	1

Primary citation

Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding. Pantoliano, M.W., Whitlow, M., Wood, J.F. et al. Biochemistry (1989) 28:7205-7213. DOI 10.1021/bi00444a012 · PubMed

Other PDB entries of the same protein (UniProt P00782 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1TO2 1.3 Å, crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59K,…
1TM5 1.45 Å, crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59A…
1LW6 1.5 Å, Crystal Structure of the Complex of Subtilisin BPN' with Chymotrypsin Inhibitor 2 at 1.5…
1V5I 1.5 Å, Crystal structure of serine protease inhibitor POIA1 in complex with subtilisin BPN'
1Y34 1.55 Å, Crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 E60A…
8H7O 1.55 Å, Crystal structure of aqualigase
1Y1K 1.56 Å, Crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 T58A…
1TM3 1.57 Å, crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59k…
1TM7 1.59 Å, crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59Y…
1SUP 1.6 Å, Subtilisin bpn' at 1.6 Å resolution: analysis of discrete disorder and comparison of…
1Y4A 1.6 Å, Crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2…
7AM3 1.61 Å, Crystal structure of Peptiligase mutant - M222P

Browse structure collections

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