1H4W: Human trypsin IV

Structure of human trypsin IV (brain trypsin). Determined by X-ray diffraction at 1.7 Å resolution. Released 11 Feb 2002.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 1,893
Mol. weight: 24.46 kDa
Ligands: BEN, CA
Released: 11 Feb 2002

Explore 1H4W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1H4W contains 8 α-helices and 20 β-strands across 1 chain. 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	30-34	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	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
α-helix	111-114	4
β-strand	122	1	2
α-helix	123-124	2
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	231-234	4
α-helix	235-244	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Trypsin iva	A	protein	224	HOMO SAPIENS	P35030 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1H4W_1 TRYPSIN IVA (chains A)
IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAHCYKTRIQVRLGEHNIKVLEG
NEQFINAVKIIRHPKYNRDTLDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISG
WGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSMFCVGFLEGGKDSCQRDSGGP
VVCNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS

Ligands and cofactors

ID	Name	Formula	Copies
BEN	Benzamidine	C7 H8 N2	1
CA	Calcium ion	Ca	1

Primary citation

Crystal structure reveals basis for the inhibitor resistance of human brain trypsin. Katona, G., Berglund, G.I., Hajdu, J. et al. J Mol Biol (2002) 315:1209-1218. DOI 10.1006/jmbi.2001.5305 · PubMed

Other PDB entries of the same protein (UniProt P35030 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5TP0 1.25 Å, Human mesotrypsin in complex with diminazene
3P95 1.3 Å, Human mesotrypsin complexed with bovine pancreatic trypsin inhibitor variant…
2R9P 1.4 Å, Human mesotrypsin complexed with bovine pancreatic trypsin inhibitor(BPTI)
4DG4 1.4 Å, Human mesotrypsin-S39Y complexed with bovine pancreatic trypsin inhibitor (BPTI)
5JBT 1.4 Å, Mesotrypsin in complex with cleaved amyloid precursor like protein 2 inhibitor (APLP2)
3P92 1.6 Å, Human mesotrypsin complexed with bovine pancreatic trypsin inhibitor variant…
9BOT 1.6 Å, Human mesotrypsin (PRSS3) unliganded and in autoinhibited (E*) conformation
4U32 1.65 Å, Human mesotrypsin complexed with HAI-2 Kunitz domain 1
9BOS 1.7 Å, Human mesotrypsin (PRSS3) unliganded and in an active (E) conformation
5C67 1.83 Å, Human Mesotrypsin in complex with amyloid precursor protein inhibitor variant…
6BX8 1.98 Å, Human Mesotrypsin (PRSS3) Complexed with Tissue Factor Pathway Inhibitor Variant…
6GFI 2.3 Å, Structure of Human Mesotrypsin in complex with APPI variant T11V/M17R/I18F/F34V

Browse structure collections

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