Atomistry » Zinc » PDB 3ciz-3cyu » 3cnq
Atomistry »
  Zinc »
    PDB 3ciz-3cyu »
      3cnq »

Zinc in PDB 3cnq: Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM

Enzymatic activity of Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM

All present enzymatic activity of Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM:
3.4.21.62;

Protein crystallography data

The structure of Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM, PDB code: 3cnq was solved by D.T.Gallagher, P.N.Bryan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.71
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.195, 72.941, 93.112, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 23.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM (pdb code 3cnq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM, PDB code: 3cnq:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in 3cnq

Go back to Zinc Binding Sites List in 3cnq
Zinc binding site 1 out of 5 in the Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM within 5.0Å range:
probe atom residue distance (Å) B Occ
S:Zn278

b:39.3
occ:1.00
O S:ALA169 2.3 11.5 1.0
O S:TYR171 2.4 14.2 1.0
O S:VAL174 2.4 13.8 1.0
O S:HOH319 2.5 20.8 1.0
C S:TYR171 3.3 15.1 1.0
C S:VAL174 3.5 13.0 1.0
C S:ALA169 3.5 11.6 1.0
C S:LYS170 3.9 14.1 1.0
N S:TYR171 3.9 14.4 1.0
CA S:PRO172 4.0 15.8 1.0
OD2 S:ASP197 4.0 21.7 1.0
N S:PRO172 4.1 15.8 1.0
N S:VAL174 4.1 13.3 1.0
CB S:ALA176 4.1 11.4 1.0
O S:PRO172 4.1 16.9 1.0
CA S:VAL174 4.1 11.7 1.0
C S:PRO172 4.1 16.5 1.0
O S:GLU195 4.1 17.8 1.0
O S:LYS170 4.2 15.1 1.0
CB S:VAL174 4.2 11.5 1.0
CA S:TYR171 4.3 15.3 1.0
CA S:LYS170 4.3 13.4 1.0
N S:ALA176 4.3 12.8 1.0
N S:LYS170 4.3 11.5 1.0
CA S:ALA169 4.5 12.5 1.0
NH2 S:ARG247 4.5 20.7 1.0
N S:ILE175 4.6 12.5 1.0
C S:ILE175 4.7 12.5 1.0
CA S:ALA176 4.7 11.6 1.0
CA S:ILE175 4.8 13.1 1.0
N S:SER173 4.8 14.8 1.0
O S:PRO168 4.9 12.2 1.0
CG1 S:VAL174 4.9 12.1 1.0
CB S:GLU195 4.9 19.6 1.0

Zinc binding site 2 out of 5 in 3cnq

Go back to Zinc Binding Sites List in 3cnq
Zinc binding site 2 out of 5 in the Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM within 5.0Å range:
probe atom residue distance (Å) B Occ
S:Zn279

b:21.0
occ:1.00
ND1 S:HIS238 2.1 16.2 1.0
O S:HOH401 2.4 8.3 1.0
CE1 S:HIS238 3.0 19.2 1.0
CG S:HIS238 3.1 15.9 1.0
CB S:HIS238 3.4 14.7 1.0
CA S:HIS238 3.5 15.3 1.0
NE1 S:TRP241 3.9 16.9 1.0
O S:LYS237 4.0 14.7 1.0
NE2 S:HIS238 4.2 16.2 1.0
CD2 S:HIS238 4.2 15.7 1.0
CD1 S:TRP241 4.4 15.9 1.0
N S:HIS238 4.5 13.7 1.0
C S:HIS238 4.5 15.7 1.0
C S:LYS237 4.6 14.2 1.0
CE2 S:TRP241 4.7 16.3 1.0
O S:HOH326 4.8 38.8 1.0
CD S:PRO239 5.0 15.9 1.0

Zinc binding site 3 out of 5 in 3cnq

Go back to Zinc Binding Sites List in 3cnq
Zinc binding site 3 out of 5 in the Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM within 5.0Å range:
probe atom residue distance (Å) B Occ
S:Zn280

b:52.7
occ:1.00
ND1 S:HIS39 2.0 26.2 1.0
OD1 S:ASP41 2.3 41.6 1.0
CE1 S:HIS39 2.9 23.8 1.0
CD S:PRO40 3.1 39.8 1.0
CG S:HIS39 3.1 30.1 1.0
N S:ASP41 3.2 42.7 1.0
CG S:ASP41 3.2 42.4 1.0
N S:PRO40 3.3 39.9 1.0
CB S:HIS39 3.5 34.5 1.0
C S:HIS39 3.7 38.0 1.0
CB S:ASP41 3.8 42.4 1.0
CA S:HIS39 3.9 35.3 1.0
CG S:PRO40 3.9 40.5 1.0
CB S:PRO40 4.0 41.0 1.0
CA S:PRO40 4.0 41.1 1.0
CA S:ASP41 4.0 41.6 1.0
NE2 S:HIS39 4.0 27.6 1.0
C S:PRO40 4.1 42.3 1.0
OH S:TYR214 4.1 38.1 1.0
N S:LEU42 4.1 39.2 1.0
CD2 S:HIS39 4.2 27.6 1.0
OD2 S:ASP41 4.2 39.4 1.0
CG2 S:THR208 4.2 21.2 1.0
CE2 S:TYR214 4.2 40.2 1.0
O S:HIS39 4.4 38.6 1.0
CZ S:TYR214 4.5 38.6 1.0
C S:ASP41 4.7 41.0 1.0

Zinc binding site 4 out of 5 in 3cnq

Go back to Zinc Binding Sites List in 3cnq
Zinc binding site 4 out of 5 in the Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM within 5.0Å range:
probe atom residue distance (Å) B Occ
S:Zn281

b:35.1
occ:1.00
ND1 S:HIS17 2.1 19.2 1.0
O S:HOH339 2.2 25.4 1.0
CE1 S:HIS17 3.0 18.1 1.0
CG S:HIS17 3.1 18.6 1.0
CB S:HIS17 3.5 16.8 1.0
NE2 S:HIS17 4.2 15.8 1.0
CD2 S:HIS17 4.2 17.7 1.0
O S:HOH532 4.6 39.3 1.0
CA S:PRO14 4.6 17.7 1.0
CB S:PRO14 4.7 18.5 1.0
CG S:PRO14 4.9 18.2 1.0

Zinc binding site 5 out of 5 in 3cnq

Go back to Zinc Binding Sites List in 3cnq
Zinc binding site 5 out of 5 in the Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Prosubtilisin Substrate Complex of Subtilisin SUBT_BACAM within 5.0Å range:
probe atom residue distance (Å) B Occ
S:Zn282

b:30.3
occ:1.00
O S:HOH473 2.0 20.7 1.0
OD2 S:ASP259 2.2 25.3 1.0
CG S:ASP259 3.1 26.6 1.0
OD1 S:ASP259 3.4 28.0 1.0
CB S:ASP259 4.4 24.8 1.0
CE2 S:TYR262 4.9 21.5 1.0

Reference:

B.Ruan, V.London, K.E.Fisher, D.T.Gallagher, P.N.Bryan. Engineering Substrate Preference in Subtilisin: Structural and Kinetic Analysis of A Specificity Mutant. Biochemistry V. 47 6628 2008.
ISSN: ISSN 0006-2960
PubMed: 18507395
DOI: 10.1021/BI800089F
Page generated: Wed Dec 16 04:11:05 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy