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Calcium in PDB 1nlu: Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin

Enzymatic activity of Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin

All present enzymatic activity of Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin:
3.4.21.100;

Protein crystallography data

The structure of Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin, PDB code: 1nlu was solved by A.Wlodawer, M.Li, A.Gustchina, Z.Dauter, K.Uchida, H.Oyama, N.E.Glodfarb, B.M.Dunn, K.Oda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.30
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 97.840, 97.840, 82.680, 90.00, 90.00, 120.00
R / Rfree (%) n/a / 19.5

Other elements in 1nlu:

The structure of Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin also contains other interesting chemical elements:

Iodine (I) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin (pdb code 1nlu). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin, PDB code: 1nlu:

Calcium binding site 1 out of 1 in 1nlu

Go back to Calcium Binding Sites List in 1nlu
Calcium binding site 1 out of 1 in the Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Pseudomonas Sedolisin (Serine-Carboxyl Proteinase) Complexed with Two Molecules of Pseudo-Iodotyrostatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:10.4
occ:1.00
OD1 A:ASP328 2.3 11.6 1.0
O A:VAL329 2.4 11.3 1.0
O A:GLY346 2.4 10.1 1.0
OD2 A:ASP348 2.4 10.0 1.0
O A:GLY344 2.4 13.1 1.0
O A:HOH502 2.4 10.6 1.0
CG A:ASP348 3.5 9.6 1.0
CG A:ASP328 3.5 12.3 1.0
C A:GLY346 3.5 9.5 1.0
C A:VAL329 3.5 11.3 1.0
C A:GLY344 3.6 11.8 1.0
N A:GLY346 3.8 11.2 1.0
N A:VAL329 3.9 10.8 1.0
OD2 A:ASP328 4.0 13.9 1.0
N A:GLY344 4.0 10.8 1.0
C A:THR345 4.1 11.3 1.0
CA A:GLY346 4.2 10.5 1.0
O A:HOH524 4.2 11.7 1.0
OD1 A:ASP348 4.2 9.7 1.0
CB A:ASP348 4.2 8.6 1.0
CA A:VAL329 4.2 10.6 1.0
O A:GLY352 4.3 8.7 1.0
C A:ASP328 4.3 13.6 1.0
OG1 A:THR351 4.4 9.0 1.0
N A:ASP348 4.4 7.8 1.0
CA A:GLY344 4.5 14.9 1.0
N A:THR345 4.5 12.4 1.0
CA A:THR345 4.5 12.9 1.0
N A:LYS330 4.5 9.9 1.0
C A:TRP347 4.6 8.3 1.0
N A:TRP347 4.6 9.1 1.0
CA A:ASP328 4.6 10.7 1.0
CB A:ASP328 4.7 10.8 1.0
CB A:VAL329 4.7 9.6 1.0
CA A:LYS330 4.7 11.7 1.0
O A:THR345 4.7 13.5 1.0
CA A:TRP347 4.8 8.5 1.0
CG A:LYS330 4.8 15.9 1.0
O A:HOH626 4.9 27.8 1.0

Reference:

A.Wlodawer, M.Li, A.Gustchina, H.Oyama, K.Oda, B.B.Beyer, J.Clemente, B.M.Dunn. Two Inhibitor Molecules Bound in the Active Site of Pseudomonas Sedolisin: A Model For the Bi-Product Complex Following Cleavage of A Peptide Substrate. Biochem.Biophys.Res.Commun. V. 314 638 2004.
ISSN: ISSN 0006-291X
PubMed: 14733955
DOI: 10.1016/J.BBRC.2003.12.130
Page generated: Sat Dec 12 03:08:56 2020

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