2XTT: Bovine trypsin

Bovine trypsin in complex with evolutionary enhanced Schistocerca gregaria protease inhibitor 1 (SGPI-1-P02). Determined by X-ray diffraction at 0.93 Å resolution. Released 10 Nov 2010.

Method: X-ray diffraction
Resolution: 0.93 Å
Organisms: SCHISTOCERCA GREGARIA, BOS TAURUS
Chains: 2
Atoms: 2,313
Mol. weight: 27.36 kDa
Ligands: CA
Released: 10 Nov 2010

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

Secondary structure: helices and β-sheets

2XTT contains 9 α-helices and 23 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: 1 helix, 3 β-strands

Element	Residues	Length	Sheet
β-strand	9-12	4	1
β-strand	15-19	5	1
β-strand	25-28	4	1
α-helix	33-35	3

Chain B: 8 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	2
β-strand	20-21	2	1
β-strand	30-34	5	3
β-strand	40-48	9	3
β-strand	51-54	4	3
α-helix	56-58	3
β-strand	64-67	4	3
β-strand	81-90	10	3
β-strand	104-108	5	3
α-helix	111-114	4
β-strand	115	1	4
β-strand	118	1	4
β-strand	122	1	1
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	1
β-strand	156-162	7	1
α-helix	163-164	2
α-helix	165-171	7
β-strand	180-183	4	1
β-strand	189	1	2
β-strand	198-201	4	1
β-strand	204-216	9	1
β-strand	221	1	5
β-strand	224	1	5
β-strand	226-230	5	1
α-helix	231-234	4
α-helix	235-244	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protease inhibitor sgpi-1	A	protein	36	SCHISTOCERCA GREGARIA	O46162 (AlphaFold model)
Cationic trypsin	B	protein	223	BOS TAURUS	P00760 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2XTT_1 PROTEASE INHIBITOR SGPI-1 (chains A)
EQECEPGQTKKQDCNTCRCGSDGVWACTRMGCPPHA

Sequence of entity 2 (B), FASTA

>2XTT_2 CATIONIC TRYPSIN (chains B)
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG
WGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGP
VVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1

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

Primary citation

The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action. Wahlgren, W.Y., Pal, G., Kardos, J. et al. J Biol Chem (2011) 286:3587-3596. DOI 10.1074/jbc.M110.161604 · PubMed

Other PDB entries of the same protein (UniProt O46162 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2F91 1.2 Å, 1.2A resolution structure of a crayfish trypsin complexed with a peptide inhibitor, SGTI
3TVJ 1.28 Å, Catalytic fragment of MASP-2 in complex with its specific inhibitor developed by…
4DJZ 3.2 Å, Catalytic fragment of masp-1 in complex with its specific inhibitor developed by…
1KGM Solution structure of the small serine protease inhibitor sgci
1KIO Solution structure of the small serine protease inhibitor SGCI[L30R, K31M]
1KJ0 Solution structure of the small serine protease inhibitor sgti

Browse structure collections

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