2SEC: Subtilisin carlsberg

Structural comparison of two serine proteinase-protein inhibitor complexes. Eglin-C-subtilisin carlsberg and ci-2-subtilisin novo. Determined by X-ray diffraction at 1.8 Å resolution. Released 7 Sept 1988.

Method: X-ray diffraction
Resolution: 1.8 Å
Organisms: Bacillus licheniformis, Hirudo medicinalis
Chains: 2
Atoms: 2,623
Mol. weight: 35.53 kDa
Ligands: CA
Released: 7 Sept 1988

Explore 2SEC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2SEC contains 15 α-helices and 25 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 E: 13 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	13-18	6
β-strand	27-32	6	1
β-strand	44-49	6	1
α-helix	64-73	10
β-strand	89-94	6	1
β-strand	101	1	2
α-helix	104-116	13
β-strand	121-124	4	1
β-strand	126-127	2	2
β-strand	128	1	3
α-helix	133-145	13
β-strand	148-152	5	1
β-strand	159	1	4
β-strand	162	1	4
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	196-201	6	1
β-strand	205-209	5	5
β-strand	213-217	5	5
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

Chain I: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	23	1	6
α-helix	25-27	3
β-strand	31	1	6
α-helix	32-42	11
β-strand	47-52	6	6
β-strand	57-58	2	2
β-strand	65-71	7	6
β-strand	75-76	2	6
β-strand	81-82	2	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Subtilisin carlsberg	E	protein	274	Bacillus licheniformis	P00780 (AlphaFold model)
Eglin C	I	protein	70	Hirudo medicinalis	P01051 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>2SEC_1 SUBTILISIN CARLSBERG (chains E)
AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDG
NGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDV
INMSLGGASGSTAMKQAVDNAYARGVVVVAAAGNSGNSGSTNTIGYPAKYDSVIAVGAVD
SNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNL
SASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ

Sequence of entity 2 (I), FASTA

>2SEC_2 EGLIN C (chains I)
TEFGSELKSFPEVVGKTVDQAREYFTLHYPQYNVYFLPEGSPVTLDLRYNRVRVFYNPGT
NVVNHVPHVG

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	3

Primary citation

Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo. McPhalen, C.A., James, M.N. Biochemistry (1988) 27:6582-6598. DOI 10.1021/bi00417a058 · 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
1SCN 1.9 Å, Inactivation of subtilisin carlsberg by N-(tert-butoxycarbonyl-alanyl-prolyl-phenylalanyl…
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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