4B2B: Factor Xa-like trypsin variant triple-Ala

Structure of the factor Xa-like trypsin variant triple-Ala (TGPA) in complex with eglin C. Determined by X-ray diffraction at 1.36 Å resolution. Released 1 Aug 2012.

Method: X-ray diffraction
Resolution: 1.36 Å
Organisms: BOS TAURUS, HIRUDO MEDICINALIS
Chains: 4
Atoms: 5,099
Mol. weight: 64.45 kDa
Ligands: CA
Released: 1 Aug 2012

Explore 4B2B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4B2B contains 21 α-helices and 56 β-strands across 4 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: 7 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
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
β-strand	122	1	2
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	2
β-strand	151	1	4
β-strand	156-162	7	2
α-helix	163-164	2
α-helix	165-170	6
β-strand	180-183	4	2
β-strand	189	1	1
β-strand	198-201	4	2
β-strand	204-217	10	2
β-strand	226-230	5	2
α-helix	231-234	4
α-helix	235-243	9

Chain B: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	4
α-helix	6-8	3
β-strand	9	1	5
α-helix	11-13	3
β-strand	17	1	6
α-helix	18-28	11
β-strand	33-38	6	5
β-strand	42-44	3	2
β-strand	51-56	6	5
β-strand	62	1	6
β-strand	63	1	5
β-strand	68-69	2	5

Chain C: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	7
β-strand	20-21	2	8
β-strand	30-34	5	9
β-strand	40-48	9	9
β-strand	51-54	4	9
α-helix	56-58	3
β-strand	64-67	4	9
β-strand	81-90	10	9
β-strand	104-108	5	9
β-strand	115	1	10
β-strand	118	1	10
β-strand	122	1	8
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	8
β-strand	151	1	11
β-strand	156-162	7	8
α-helix	163-164	2
α-helix	165-170	6
β-strand	180-183	4	8
β-strand	189	1	7
β-strand	198-201	4	8
β-strand	204-217	10	8
β-strand	221A	1	12
β-strand	224	1	12
β-strand	226-230	5	8
α-helix	231-234	4
α-helix	235-244	10

Chain D: 4 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	11
α-helix	6-8	3
β-strand	9	1	13
α-helix	11-13	3
β-strand	17	1	14
α-helix	18-28	11
β-strand	33-38	6	13
β-strand	42-44	3	8
β-strand	51-56	6	13
β-strand	62	1	14
β-strand	63	1	13
α-helix	66-67	2
β-strand	68-69	2	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cationic trypsin	A, C	protein	223	BOS TAURUS	P00760 (AlphaFold model)
Eglin C	B, D	protein	71	HIRUDO MEDICINALIS	P01051 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>4B2B_1 CATIONIC TRYPSIN (chains A, C)
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSETYNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG
WGNTKSSGTSYPDVLKCLKAPILSDSSCKSASSFIITSNMFCAGYLEGGKDACQGDAGGP
VVCSGKLQGIVSWGEGCAQKNKPGFYTKVCNYVSWIKQTIASN

Sequence of entity 2 (B, D), FASTA

>4B2B_2 EGLIN C (chains B, D)
GTEFGSELKSFPEVVGKTVDQAREYFTLHYPQYDVYFLPEGSPVTKDLRYNRVRVFYNPG
TNVVNHVPHVG

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2

Water and common crystallization additives (GOL, EDO, CL) are not listed.

Primary citation

Thermodynamic signatures in macromolecular interactions involving conformational flexibility. Menzel, A., Neumann, P., Schwieger, C. et al. Biol Chem (2014) 395:905-911. DOI 10.1515/hsz-2014-0177 · PubMed

Other PDB entries of the same protein (UniProt P00760 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4I8H 0.75 Å, Bovine trypsin at 0.75 resolution
5MN1 0.79 Å, Cationic trypsin in complex with 2-aminopyridine (deuterated sample at 100 K)
5MNK 0.8 Å, Cationic trypsin in complex with benzylamine (deuterated sample at 100 K)
3MFJ 0.8 Å, Bovine trypsin at 0.8 A resolution, restrained refinement
3MI4 0.8 Å, Bovine trypsin at 0.8 A resolution, non-restrained refinement
4I8G 0.8 Å, Bovine trypsin at 0.8 resolution
4I8K 0.85 Å, Bovine trypsin at 0.85 resolution
5MNN 0.86 Å, Cationic trypsin in complex with N-amidinopiperidine (deuterated sample at 100 K)
5MNG 0.86 Å, Cationic trypsin in complex with benzamidine (deuterated sample at 100 K)
4I8J 0.87 Å, Bovine trypsin at 0.87 A resolution
4I8L 0.87 Å, Bovine trypsin at 0.87 resolution
4XOJ 0.91 Å, Structure of bovine trypsin in complex with analogues of sunflower inhibitor 1 (SFTI-1)

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