1SCN: Subtilisin carlsberg

Inactivation of subtilisin carlsberg by N-(tert-butoxycarbonyl-alanyl-prolyl-phenylalanyl)-O-benzol hydroxylamine: formation of covalent enzyme-inhibitor linkage in the form of a carbamate derivative. Determined by X-ray diffraction at 1.9 Å resolution. Released 31 Aug 1994.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Bacillus licheniformis
Chains: 1
Atoms: 2,094
Mol. weight: 28.03 kDa
Ligands: 0EF, CA
Released: 31 Aug 1994

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

Secondary structure: helices and β-sheets

1SCN 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 E: 11 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	13-17	5
β-strand	27-32	6	1
β-strand	44-49	6	1
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	2
α-helix	133-144	12
β-strand	148-152	5	1
β-strand	159	1	3
β-strand	162	1	3
β-strand	167	1	2
β-strand	175-180	6	1
β-strand	186	1	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
α-helix	254	1
β-strand	255	1	1
α-helix	256	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 carlsberg	E	protein	276	Bacillus licheniformis	P00780 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>1SCN_1 SUBTILISIN CARLSBERG (chains E)
AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDG
NGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDV
INMSLGGASGSTAMKQAVDNAYARGVVVVAAAGNSGNSGSTNTIGYPAKYDSVIAVGAVD
SNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNL
SASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQAP

Ligands and cofactors

ID	Name	Formula	Copies
0EF	N-(tert-butoxycarbonyl)-L-alanyl-N-[(1R)-1-(carboxyamino)-2-phenylethyl]-L-prol…	C22 H32 N4 O6	1
CA	Calcium ion	Ca	2

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

Primary citation

Inactivation of subtilisin Carlsberg by N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-benzolhydroxyl- amine: formation of a covalent enzyme-inhibitor linkage in the form of a carbamate derivative. Steinmetz, A.C., Demuth, H.U., Ringe, D. Biochemistry (1994) 33:10535-10544. DOI 10.1021/bi00200a040 · PubMed

Other PDB entries of the same protein (UniProt P00780 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1R0R 1.1 Å, 1.1 Angstrom Resolution Structure of the Complex Between the Protein Inhibitor, OMTKY3,…
1CSE 1.2 Å, The high-resolution X-ray crystal structure of the complex formed between subtilisin…
3UNX 1.26 Å, Bond length analysis of asp, glu and his residues in subtilisin Carlsberg at 1.26A…
6DWQ 1.27 Å, Subtilisin serine protease modified with the protease inhibitor…
1YU6 1.55 Å, Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex
2SEC 1.8 Å, Structural comparison of two serine proteinase-protein inhibitor complexes.…
1AVT 2.0 Å, Subtilisin carlsberg D-para-chlorophenyl-1-acetamido boronic acid inhibitor complex
1SCA 2.0 Å, Enzyme crystal structure in a neat organic solvent
1SEL 2.0 Å, Crystal structure of selenosubtilisin at 2.0-Å resolution
1VSB 2.1 Å, Subtilisin carlsberg L-para-chlorophenyl-1-acetamido boronic acid inhibitor complex
1BE6 2.15 Å, Trans-cinnamoyl-subtilisin in anhydrous acetonitrile
1C3L 2.16 Å, Subtilisin-carlsberg complexed with xenon (8 bar)

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