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Calcium in PDB 6m9d: Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Chymostatin

Enzymatic activity of Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Chymostatin

All present enzymatic activity of Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Chymostatin:
3.4.21.100;

Protein crystallography data

The structure of Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Chymostatin, PDB code: 6m9d was solved by A.Wlodawer, M.Li, A.Gustchina, Z.Dauter, K.Uchida, H.Oyama, N.E.Goldfarb, B.M.Dunn, K.Oda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.00
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 98.570, 98.570, 83.390, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / 25.1

Calcium Binding Sites:

The binding sites of Calcium atom in the Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Chymostatin (pdb code 6m9d). 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 Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Chymostatin, PDB code: 6m9d:

Calcium binding site 1 out of 1 in 6m9d

Go back to Calcium Binding Sites List in 6m9d
Calcium binding site 1 out of 1 in the Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Chymostatin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Pseudomonas Serine-Carboxyl Proteinase (Sedolisin) Complexed with the Inhibitor Chymostatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca390

b:28.3
occ:1.00
 OD1 A:ASP328 2.2 21.9 1.0
O A:VAL329 2.3 33.6 1.0
O A:GLY344 2.3 20.1 1.0
OD2 A:ASP348 2.3 25.2 1.0
O A:GLY346 2.4 23.7 1.0
O A:HOH401 2.6 23.4 1.0
H A:GLY344 3.2 31.9 1.0
CG A:ASP328 3.4 27.6 1.0
CG A:ASP348 3.5 28.2 1.0
C A:VAL329 3.5 30.9 1.0
C A:GLY346 3.5 27.2 1.0
C A:GLY344 3.5 25.9 1.0
H A:VAL329 3.7 33.5 1.0
N A:VAL329 3.9 27.9 1.0
N A:GLY346 3.9 21.8 1.0
H A:GLY346 3.9 26.1 1.0
OD2 A:ASP328 3.9 21.5 1.0
HA A:LYS330 4.0 35.9 1.0
N A:GLY344 4.0 26.6 1.0
HG1 A:THR351 4.0 34.1 1.0
HB3 A:ASP348 4.0 28.5 1.0
HB A:VAL329 4.1 26.9 1.0
O A:HOH423 4.1 18.8 1.0
CA A:GLY346 4.2 27.4 1.0
HB1 A:ALA343 4.2 36.9 1.0
CA A:VAL329 4.2 28.7 1.0
C A:THR345 4.2 26.9 1.0
HA A:THR345 4.3 32.4 1.0
O A:GLY352 4.3 22.5 1.0
OD1 A:ASP348 4.3 29.5 1.0
HA A:ASP328 4.3 33.2 1.0
H A:ASP348 4.3 28.5 1.0
HG2 A:LYS330 4.3 56.8 1.0
CB A:ASP348 4.3 23.7 1.0
C A:ASP328 4.3 27.7 1.0
OG1 A:THR351 4.4 22.8 1.0
CA A:GLY344 4.4 25.0 1.0
HG3 A:LYS330 4.4 56.8 1.0
HA2 A:GLY346 4.4 32.9 1.0
N A:ASP348 4.4 23.7 1.0
N A:THR345 4.5 23.1 1.0
N A:LYS330 4.5 26.5 1.0
HA A:TRP347 4.5 21.6 1.0
CA A:THR345 4.6 27.0 1.0
N A:TRP347 4.6 18.1 1.0
CB A:ASP328 4.6 26.8 1.0
C A:TRP347 4.6 22.5 1.0
CA A:ASP328 4.6 27.7 1.0
CB A:VAL329 4.7 22.4 1.0
CA A:LYS330 4.7 29.9 1.0
O A:THR345 4.7 27.5 1.0
CA A:TRP347 4.8 18.0 1.0
CG A:LYS330 4.8 47.4 1.0
HG11 A:VAL329 4.9 45.2 1.0
HA A:ALA343 5.0 28.5 1.0
O A:ASP328 5.0 27.1 1.0

Reference:

A.Wlodawer, M.Li, A.Gustchina, Z.Dauter, K.Uchida, H.Oyama, N.E.Goldfarb, B.M.Dunn, K.Oda. Inhibitor Complexes of the Pseudomonas Serine-Carboxyl Proteinase Biochemistry V. 40 15602 2001.
ISSN: ISSN 0006-2960
PubMed: 11747435
DOI: 10.1021/BI011817N
Page generated: Tue Jul 16 11:16:46 2024

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