1U0O: Botrocetin

The mouse von Willebrand Factor A1-botrocetin complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 19 Apr 2005.

Method: X-ray diffraction
Resolution: 2.7 Å
Organisms: Bothrops jararaca, Mus musculus
Chains: 3
Atoms: 3,728
Mol. weight: 53.85 kDa
Released: 19 Apr 2005

Explore 1U0O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1U0O contains 14 α-helices and 29 β-strands across 3 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: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	7-8	2	1
β-strand	13-21	9	1
α-helix	23-30	8
β-strand	38-39	2	1
α-helix	47-59	13
β-strand	66-73	8	1
β-strand	83	1	2
β-strand	89	1	2
β-strand	95	1	3
β-strand	103-107	5	1
α-helix	109-112	4
β-strand	114-118	5	1
β-strand	124-130	7	1

Chain B: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	202-203	2
β-strand	207-209	3	3
β-strand	212-221	10	3
α-helix	223-231	9
β-strand	238-239	2	3
α-helix	245-254	10
β-strand	264-265	2	3
β-strand	277-279	3	1
α-helix	287-290	4
β-strand	297-302	6	3
β-strand	307-312	6	3
β-strand	317-323	7	3

Chain C: 7 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	509	1	4
β-strand	513-520	8	5
β-strand	522	1	6
α-helix	527-541	15
β-strand	544	1	4
β-strand	546	1	5
β-strand	551-558	8	5
β-strand	562-566	5	5
α-helix	574-582	9
β-strand	589	1	6
α-helix	594-603	10
β-strand	615-622	8	5
α-helix	628-631	4
α-helix	634-643	10
β-strand	646-653	8	5
α-helix	659-667	9
β-strand	675-677	3	5
α-helix	680-695	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Botrocetin	A	protein	133	Bothrops jararaca	P22029 (AlphaFold model)
Botrocetin	B	protein	125	Bothrops jararaca	P22030 (AlphaFold model)
von Willebrand factor	C	protein	208	Mus musculus	Q8CIZ8 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1U0O_1 Botrocetin (chains A)
DCPSGWSSYEGNCYKFFQQKMNWADAERFCSEQAKGGHLVSIKIYSKEKDFVGDLVTKNI
QSSDLYAWIGLRVENKEKQCSSEWSDGSSVSYENVVERTVKKCFALEKDLGFVLWINLYC
AQKNPFVCKSPPP

Sequence of entity 2 (B), FASTA

>1U0O_2 Botrocetin (chains B)
DCPPDWSSYEGHCYRFFKEWMHWDDAEEFCTEQQTGAHLVSFQSKEEADFVRSLTSEMLK
GDVVWIGLSDVWNKCRFEWTDGMEFDYDDYYLIAEYECVASKPTNNKWWIIPCTRFKNFV
CEFQA

Sequence of entity 3 (C), FASTA

>1U0O_3 von Willebrand factor (chains C)
DTPEPPLHNFYCSKLLDLVFLLDGSSMLSEAEFEVLKAFVVGMMERLHISQKRIRVAVVE
YHDGSRAYLELKARKRPSELRRITSQIKYTGSQVASTSEVLKYTLFQIFGKIDRPEASHI
TLLLTASQEPPRMARNLVRYVQGLKKKKVIVIPVGIGPHASLKQIRLIEKQAPENKAFLL
SGVDELEQRRDEIVSYLCDLAPEAPAPT

Primary citation

The snake venom protein botrocetin acts as a biological brace to promote dysfunctional platelet aggregation. Fukuda, K., Doggett, T., Laurenzi, I.J. et al. Nat Struct Mol Biol (2005) 12:152-159. DOI 10.1038/nsmb892 · PubMed

Other PDB entries of the same protein (UniProt P22029 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1FVU 1.8 Å, Crystal structure of botrocetin
1IJK 2.6 Å, The von Willebrand Factor mutant (I546V) A1 domain-botrocetin Complex
1U0N 2.95 Å, The ternary von Willebrand Factor A1-glycoprotein Ibalpha-botrocetin complex

Browse structure collections

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