1AVW: Trypsin

Complex porcine pancreatic trypsin/soybean trypsin inhibitor, orthorhombic crystal form. Determined by X-ray diffraction at 1.75 Å resolution. Released 28 Oct 1998.

Method: X-ray diffraction
Resolution: 1.75 Å
Organisms: Sus scrofa, Glycine max
Chains: 2
Atoms: 3,042
Mol. weight: 43.19 kDa
Ligands: CA
Released: 28 Oct 1998

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

Secondary structure: helices and β-sheets

1AVW contains 13 α-helices and 42 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: 8 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-37	6	3
β-strand	39-48	10	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	95	1	5
β-strand	100	1	5
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	154	1	4
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	226-230	5	2
α-helix	231-233	3
α-helix	235-244	10

Chain B: 5 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	502	1	6
β-strand	504	1	7
α-helix	509	1
β-strand	510	1	7
α-helix	511	1
β-strand	512	1	8
β-strand	515-521	7	9
β-strand	529-532	4	10
β-strand	542-545	4	10
β-strand	556-559	4	9
β-strand	562	1	2
β-strand	566	1	8
β-strand	568	1	6
β-strand	573-577	5	9
α-helix	578-579	2
α-helix	584-586	3
β-strand	592	1	9
β-strand	594-596	3	10
β-strand	604-606	3	10
β-strand	613	1	10
α-helix	614-615	2
β-strand	616-622	7	9
β-strand	631-637	7	9
β-strand	646-647	2	9
β-strand	648-652	5	10
β-strand	659-663	5	10
β-strand	670-675	6	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Trypsin	A	protein	223	Sus scrofa	P00761 (AlphaFold model)
Trypsin inhibitor	B	protein	177	Glycine max	P01070 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1AVW_1 TRYPSIN (chains A)
IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEG
NEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISG
WGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGP
VVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN

Sequence of entity 2 (B), FASTA

>1AVW_2 TRYPSIN INHIBITOR (chains B)
DFVLDNEGNPLENGGTYYILSDITAFGGIRAAPTGNERCPLTVVQSRNELDKGIGTIISS
PYRIRFIAEGHPLSLKFDSFAVIMLCVGIPTEWSVVEDLPEGPAVKIGENKDAMDGWFRL
ERVSDDEFNNYKLVFCPQQAEDDKCGDIGISIDHDDGTRRLVVSKNKPLVVQFQKLD

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1

Primary citation

Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator. Song, H.K., Suh, S.W. J Mol Biol (1998) 275:347-363. DOI 10.1006/jmbi.1997.1469 · 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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