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Vanadium in PDB 2p8o: Crystal Structure of A Benzohydroxamic Acid/Vanadate Complex Bound to Chymotrypsin A

Enzymatic activity of Crystal Structure of A Benzohydroxamic Acid/Vanadate Complex Bound to Chymotrypsin A

All present enzymatic activity of Crystal Structure of A Benzohydroxamic Acid/Vanadate Complex Bound to Chymotrypsin A:
3.4.21.1;

Protein crystallography data

The structure of Crystal Structure of A Benzohydroxamic Acid/Vanadate Complex Bound to Chymotrypsin A, PDB code: 2p8o was solved by A.Moulin, J.H.Bell, R.F.Pratt, D.Ringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.50
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 68.989, 68.989, 95.892, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 24.3

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of A Benzohydroxamic Acid/Vanadate Complex Bound to Chymotrypsin A (pdb code 2p8o). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total only one binding site of Vanadium was determined in the Crystal Structure of A Benzohydroxamic Acid/Vanadate Complex Bound to Chymotrypsin A, PDB code: 2p8o:

Vanadium binding site 1 out of 1 in 2p8o

Go back to Vanadium Binding Sites List in 2p8o
Vanadium binding site 1 out of 1 in the Crystal Structure of A Benzohydroxamic Acid/Vanadate Complex Bound to Chymotrypsin A


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Crystal Structure of A Benzohydroxamic Acid/Vanadate Complex Bound to Chymotrypsin A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:V300

b:24.2
occ:1.00
V16 C:BVA300 0.0 24.2 1.0
O9 C:BVA300 1.8 21.0 1.0
O11 C:BVA300 1.9 38.4 1.0
O8 C:BVA300 1.9 24.5 1.0
O12 C:BVA300 1.9 24.4 1.0
O10 C:BVA300 2.0 24.1 1.0
OG C:SER195 2.0 19.8 1.0
N13 C:BVA300 2.6 27.1 1.0
C14 C:BVA300 2.7 22.6 1.0
CB C:SER195 3.0 17.9 1.0
CA C:SER195 3.9 13.9 1.0
N C:SER195 3.9 13.0 1.0
O C:HOH549 4.0 37.1 1.0
NE2 B:HIS57 4.0 19.7 1.0
C15 C:BVA300 4.1 19.6 1.0
CA C:MET192 4.2 17.0 1.0
N C:GLY193 4.3 13.2 1.0
O C:HOH582 4.4 40.1 1.0
O C:CYS191 4.4 17.3 1.0
C17 C:BVA300 4.8 23.0 1.0
CG C:MET192 4.8 22.4 1.0
N C:MET192 4.8 15.9 1.0
C C:MET192 4.8 13.7 1.0
C C:CYS191 4.8 20.0 1.0
O B:HOH594 4.8 44.3 1.0
CE1 B:HIS57 4.8 19.2 1.0
O C:SER214 4.9 21.3 1.0
N C:ASP194 4.9 15.7 1.0
O C:HOH529 4.9 36.2 1.0
CD2 B:HIS57 4.9 19.0 1.0

Reference:

A.Moulin, J.H.Bell, R.F.Pratt, D.Ringe. Inhibition of Chymotrypsin By A Complex of Ortho-Vanadate and Benzohydroxamic Acid: Structure of the Inert Complex and Its Mechanistic Interpretation. Biochemistry V. 46 5982 2007.
ISSN: ISSN 0006-2960
PubMed: 17469803
DOI: 10.1021/BI6025209
Page generated: Thu Oct 29 07:04:51 2020

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