2P8O: Benzohydroxamic Acid/Vanadate complex

Crystal Structure of a Benzohydroxamic Acid/Vanadate complex bound to chymotrypsin A. Determined by X-ray diffraction at 1.5 Å resolution. Released 8 May 2007.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Bos taurus
Chains: 3
Atoms: 1,962
Mol. weight: 25.6 kDa
Ligands: BVA
Released: 8 May 2007

Explore 2P8O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2P8O 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 B: 4 helices, 15 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	65-68	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	115	1	6
β-strand	118	1	6
α-helix	120-121	2
β-strand	122	1	2
α-helix	123-125	3
β-strand	135-140	6	2

Chain C: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	154	1	4
β-strand	156-162	7	2
α-helix	163-164	2
α-helix	165-172	8
α-helix	173-175	3
β-strand	180-184	5	2
β-strand	189	1	1
β-strand	198-203	6	2
β-strand	206-215	10	2
β-strand	225-230	6	2
α-helix	231-233	3
α-helix	235-244	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chymotrypsin A chain A	A	protein	13	Bos taurus	P00766 (AlphaFold model)
Chymotrypsin A chain B	B	protein	131	Bos taurus	P00766 (AlphaFold model)
Chymotrypsin A chain C	C	protein	97	Bos taurus	P00766 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2P8O_1 Chymotrypsin A chain A (chains A)
CGVPAIQPVLSGL

Sequence of entity 2 (B), FASTA

>2P8O_2 Chymotrypsin A chain B (chains B)
IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGS
SSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTT
CVTTGWGLTRY

Sequence of entity 3 (C), FASTA

>2P8O_3 Chymotrypsin A chain C (chains C)
ANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWT
LVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN

Ligands and cofactors

ID	Name	Formula	Copies
BVA	Trihydroxy[(n-hydroxybenzamidato)oxo]vanadate	C7 H9 N O5 V	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Inhibition of chymotrypsin by a complex of ortho-vanadate and benzohydroxamic Acid: structure of the inert complex and its mechanistic interpretation. Moulin, A., Bell, J.H., Pratt, R.F. et al. Biochemistry (2007) 46:5982-5990. DOI 10.1021/bi6025209 · PubMed

Other PDB entries of the same protein (UniProt P00766 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5R43 1.0 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 7.5, cryo temperature
5R42 1.05 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 7.5, room temperature
5R44 1.05 Å, Crystal Structure of gamma-Chymotrypsin at pH 7.5, room temperature
5R45 1.05 Å, Crystal Structure of gamma-Chymotrypsin at pH 7.5, cryo temperature
5R46 1.05 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 5.6, room temperature
5R48 1.05 Å, Crystal Structure of gamma-Chymotrypsin at pH 5.6, room temperature
5R49 1.05 Å, Crystal Structure of gamma-Chymotrypsin at pH 5.6, cryo temperature
5R4B 1.05 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 9, cryo temperature
5R4D 1.05 Å, Crystal Structure of gamma-Chymotrypsin at pH 9, cryo temperature
5R47 1.1 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 5.6, cryo temperature
5R4C 1.15 Å, Crystal Structure of gamma-Chymotrypsin at pH 9, room temperature
5R4A 1.2 Å, Crystal Structure of deuterated gamma-Chymotrypsin at pH 9, room temperature

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