1AKS: Alpha trypsin

Crystal structure of the first active autolysate form of the porcine alpha trypsin. Determined by X-ray diffraction at 1.8 Å resolution. Released 12 Feb 1997.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Sus scrofa
Chains: 2
Atoms: 1,755
Mol. weight: 23.55 kDa
Ligands: CA
Released: 12 Feb 1997

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

Secondary structure: helices and β-sheets

1AKS contains 9 α-helices and 22 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: 4 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-34	5	3
β-strand	40-46	7	3
β-strand	51-54	4	3
α-helix	56-58	3
β-strand	64-67	4	3
β-strand	72	1	4
β-strand	81-90	10	3
β-strand	104-108	5	3
β-strand	115	1	5
β-strand	118	1	5
β-strand	122	1	2
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	2

Chain B: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	154	1	4
α-helix	155	1
β-strand	156-162	7	2
α-helix	163-164	2
α-helix	165-171	7
β-strand	180-183	4	2
β-strand	189	1	1
β-strand	198-201	4	2
β-strand	204-215	8	2
β-strand	221	1	6
β-strand	224	1	6
β-strand	226-230	5	2
α-helix	231-233	3
α-helix	235-244	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha trypsin	A	protein	125	Sus scrofa	P00761 (AlphaFold model)
Alpha trypsin	B	protein	98	Sus scrofa	P00761 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1AKS_1 ALPHA TRYPSIN (chains A)
IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEG
NEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISG
WGNTK

Sequence of entity 2 (B), FASTA

>1AKS_2 ALPHA TRYPSIN (chains B)
SSGSSYPSLLQCLKAPVLSNSSCKSSYPGQITGNMICVGFLQGGKDSCQGDSGGPVVCNG
QLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1

Primary citation

The first structure at 1.8 A resolution of an active autolysate form of porcine alpha-trysoin. Johnson, A., Krishnaswamy, S., Sundaram, P.V. et al. Acta Crystallogr D Biol Crystallogr (1997) 53:311-315. DOI 10.1107/S0907444997000358 · PubMed

Other PDB entries of the same protein (UniProt P00761 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9PDA 1.18 Å, Structure of Porcine Trypsin Crystals Grown From PEG and Complexed With Crystallization…
1S83 1.25 Å, Porcine trypsin complexed with 4-amino propanol
2A31 1.25 Å, Trypsin in complex with borate
9PDC 1.27 Å, Porcine Trypsin grown from PEG and Complexed with Crystallization Additives II
9PD9 1.28 Å, The Structure of Porcine Trypsin in Complex with Crystallization Additives I
1S5S 1.4 Å, Porcine trypsin complexed with guanidine-3-propanol inhibitor
9PCT 1.41 Å, Structure of Porcine Trypsin Crystals Grown from PEG Complexed with Crystallization…
1S6H 1.45 Å, Porcine trypsin complexed with guanidine-3-propanol inhibitor
1H9H 1.5 Å, Complex of eeti-II with porcine trypsin
2A32 1.5 Å, Trypsin in complex with benzene boronic acid
1FNI 1.6 Å, Crystal structure of porcine beta trypsin with 0.01% polydocanol
1MCT 1.6 Å, The refined 1.6 Å resolution crystal structure of the complex formed between porcine…

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