Atomistry » Zinc » PDB 6h51-6hc8 » 6hc6
Atomistry »
  Zinc »
    PDB 6h51-6hc8 »
      6hc6 »

Zinc in PDB 6hc6: The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis

Enzymatic activity of The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis

All present enzymatic activity of The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis:
3.4.11.10; 3.4.11.6;

Protein crystallography data

The structure of The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis, PDB code: 6hc6 was solved by E.Rogoulenko, S.Lansky, R.Faygenboim, T.Cohen, R.Alhadeff, Y.Shoham, G.Shoham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.70 / 1.77
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 224.922, 224.922, 42.502, 90.00, 90.00, 120.00
R / Rfree (%) 16.5 / 20.3

Zinc Binding Sites:

The binding sites of Zinc atom in the The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis (pdb code 6hc6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis, PDB code: 6hc6:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 6hc6

Go back to Zinc Binding Sites List in 6hc6
Zinc binding site 1 out of 6 in the The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:19.4
occ:1.00
 O A:HOH767 2.0 22.3 1.0
OD1 A:ASP262 2.0 15.7 1.0
O A:HOH611 2.1 18.7 1.0
OD1 A:ASP323 2.1 16.7 1.0
NE2 A:HIS250 2.2 11.6 1.0
OD2 A:ASP323 2.2 18.9 1.0
CG A:ASP323 2.5 17.7 1.0
CG A:ASP262 3.1 19.0 1.0
CD2 A:HIS250 3.1 15.7 1.0
CE1 A:HIS250 3.2 14.8 1.0
OD2 A:ASP262 3.6 15.0 1.0
ZN A:ZN502 3.8 21.5 1.0
CB A:ASP323 4.0 19.4 1.0
OE2 A:GLU294 4.0 17.1 1.0
OE2 A:GLU452 4.1 23.5 1.0
CB A:ASN263 4.1 13.3 1.0
OE2 A:GLU295 4.2 15.1 1.0
ND1 A:HIS250 4.3 14.0 1.0
CG A:HIS250 4.3 11.9 1.0
CB A:ASP262 4.3 20.0 1.0
O A:HOH739 4.4 33.3 1.0
CD A:GLU294 4.4 23.9 1.0
SD A:MET324 4.6 22.1 1.0
CG A:ASN263 4.6 15.0 1.0
CA A:ASP262 4.6 17.8 1.0
OE1 A:GLU294 4.6 21.4 1.0
CG A:MET324 4.6 19.5 1.0
OE1 A:GLU452 4.7 22.3 1.0
OG A:SER371 4.8 19.2 1.0
CA A:ASP323 4.8 16.2 1.0
CD A:GLU452 4.8 23.6 1.0
CD A:GLU295 4.9 17.2 1.0
ND2 A:ASN263 4.9 15.1 1.0
C A:ASP262 4.9 17.0 1.0

Zinc binding site 2 out of 6 in 6hc6

Go back to Zinc Binding Sites List in 6hc6
Zinc binding site 2 out of 6 in the The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:21.5
occ:1.00
 OD2 A:ASP262 2.0 15.0 1.0
NE2 A:HIS401 2.1 15.2 1.0
OE2 A:GLU295 2.2 15.1 1.0
OE1 A:GLU452 2.3 22.3 1.0
O A:HOH611 2.3 18.7 1.0
OE1 A:GLU295 2.3 15.8 1.0
CD A:GLU295 2.6 17.2 1.0
CE1 A:HIS401 3.0 19.9 1.0
CG A:ASP262 3.1 19.0 1.0
CD2 A:HIS401 3.2 15.6 1.0
CD A:GLU452 3.2 23.6 1.0
OD1 A:ASP262 3.4 15.7 1.0
OE2 A:GLU452 3.4 23.5 1.0
O A:HOH767 3.7 22.3 1.0
ZN A:ZN501 3.8 19.4 1.0
CE1 A:TYR400 3.9 26.9 1.0
O A:HOH686 4.0 15.4 1.0
OH A:TYR400 4.1 28.6 1.0
CG A:GLU295 4.1 13.4 1.0
ND1 A:HIS401 4.2 17.9 1.0
CG A:HIS401 4.3 15.0 1.0
OE2 A:GLU294 4.3 17.1 1.0
CZ A:TYR400 4.3 30.1 1.0
CG1 A:VAL254 4.4 17.1 1.0
CB A:ASP262 4.4 20.0 1.0
O A:HOH710 4.5 23.1 1.0
CG A:GLU452 4.6 22.5 1.0
CE1 A:HIS250 4.7 14.8 1.0
NE2 A:HIS250 4.7 11.6 1.0
CD1 A:TYR400 4.8 22.9 1.0
CB A:GLU452 5.0 26.7 1.0

Zinc binding site 3 out of 6 in 6hc6

Go back to Zinc Binding Sites List in 6hc6
Zinc binding site 3 out of 6 in the The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:18.4
occ:1.00
 OD1 B:ASP262 2.0 14.9 1.0
O B:HOH864 2.1 18.9 1.0
OD1 B:ASP323 2.2 13.3 1.0
O B:HOH612 2.2 14.8 1.0
NE2 B:HIS250 2.2 13.1 1.0
OD2 B:ASP323 2.2 17.2 1.0
CG B:ASP323 2.5 15.3 1.0
CG B:ASP262 3.1 17.7 1.0
CE1 B:HIS250 3.2 17.3 1.0
CD2 B:HIS250 3.2 12.1 1.0
OD2 B:ASP262 3.5 15.4 1.0
ZN B:ZN502 3.8 20.0 1.0
CB B:ASP323 4.0 17.4 1.0
OE2 B:GLU452 4.0 20.9 1.0
OE2 B:GLU294 4.1 15.3 1.0
CB B:ASN263 4.1 13.4 1.0
ND1 B:HIS250 4.3 13.3 1.0
CB B:ASP262 4.3 16.2 1.0
OE1 B:GLU295 4.3 14.3 1.0
CG B:HIS250 4.3 9.7 1.0
O B:HOH776 4.4 25.4 1.0
CD B:GLU294 4.5 17.7 1.0
CG B:MET324 4.5 12.6 1.0
SD B:MET324 4.5 17.2 1.0
OE1 B:GLU452 4.6 20.2 1.0
CA B:ASP262 4.6 14.8 1.0
OE1 B:GLU294 4.6 19.0 1.0
CG B:ASN263 4.6 15.0 1.0
CD B:GLU452 4.7 22.1 1.0
OG B:SER371 4.8 16.0 1.0
CA B:ASP323 4.8 16.1 1.0
C B:ASP262 4.9 15.6 1.0
CD B:GLU295 5.0 15.1 1.0
ND2 B:ASN263 5.0 14.7 1.0

Zinc binding site 4 out of 6 in 6hc6

Go back to Zinc Binding Sites List in 6hc6
Zinc binding site 4 out of 6 in the The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn502

b:20.0
occ:1.00
 OD2 B:ASP262 2.1 15.4 1.0
NE2 B:HIS401 2.1 13.5 1.0
OE1 B:GLU295 2.2 14.3 1.0
OE1 B:GLU452 2.3 20.2 1.0
O B:HOH612 2.3 14.8 1.0
OE2 B:GLU295 2.4 15.2 1.0
CD B:GLU295 2.6 15.1 1.0
CE1 B:HIS401 3.0 13.2 1.0
CG B:ASP262 3.1 17.7 1.0
CD B:GLU452 3.2 22.1 1.0
CD2 B:HIS401 3.2 15.3 1.0
OD1 B:ASP262 3.4 14.9 1.0
OE2 B:GLU452 3.5 20.9 1.0
O B:HOH864 3.7 18.9 1.0
ZN B:ZN501 3.8 18.4 1.0
CE1 B:TYR400 3.8 13.8 1.0
OH B:TYR400 4.0 19.9 1.0
O B:HOH659 4.0 14.6 1.0
CG B:GLU295 4.1 13.2 1.0
ND1 B:HIS401 4.2 16.6 1.0
CZ B:TYR400 4.3 19.0 1.0
CG B:HIS401 4.3 12.6 1.0
OE2 B:GLU294 4.3 15.3 1.0
CG1 B:VAL254 4.4 15.5 1.0
CB B:ASP262 4.4 16.2 1.0
O B:HOH689 4.5 20.1 1.0
CG B:GLU452 4.5 21.5 1.0
CE1 B:HIS250 4.7 17.3 1.0
NE2 B:HIS250 4.7 13.1 1.0
CB B:GLU452 4.8 22.8 1.0
CD1 B:TYR400 4.8 19.0 1.0

Zinc binding site 5 out of 6 in 6hc6

Go back to Zinc Binding Sites List in 6hc6
Zinc binding site 5 out of 6 in the The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn501

b:19.2
occ:1.00
 O C:HOH649 2.0 18.7 1.0
OD1 C:ASP262 2.1 16.0 1.0
OD2 C:ASP323 2.2 14.9 1.0
NE2 C:HIS250 2.2 15.2 1.0
O C:HOH851 2.2 18.2 1.0
OD1 C:ASP323 2.3 17.9 1.0
CG C:ASP323 2.5 18.5 1.0
CG C:ASP262 3.1 14.4 1.0
CE1 C:HIS250 3.1 16.9 1.0
CD2 C:HIS250 3.2 14.1 1.0
OD2 C:ASP262 3.5 17.2 1.0
ZN C:ZN502 3.8 21.5 1.0
OE2 C:GLU294 4.0 18.5 1.0
CB C:ASP323 4.1 16.8 1.0
CB C:ASN263 4.2 14.0 1.0
OE2 C:GLU452 4.2 23.7 1.0
ND1 C:HIS250 4.2 13.7 1.0
OE1 C:GLU295 4.3 16.9 1.0
CG C:HIS250 4.3 13.6 1.0
O C:HOH696 4.3 30.3 1.0
CB C:ASP262 4.3 14.9 1.0
O C:HOH818 4.3 46.2 1.0
CD C:GLU294 4.4 20.1 1.0
CG C:MET324 4.5 16.4 1.0
OE1 C:GLU294 4.6 20.1 1.0
SD C:MET324 4.6 20.3 1.0
CG C:ASN263 4.6 19.2 1.0
CA C:ASP262 4.6 13.5 1.0
OE1 C:GLU452 4.7 18.1 1.0
OG C:SER371 4.8 16.9 1.0
CD C:GLU452 4.8 23.9 1.0
CA C:ASP323 4.8 16.7 1.0
ND2 C:ASN263 4.9 11.9 1.0
C C:ASP262 4.9 16.9 1.0
CD C:GLU295 4.9 18.7 1.0

Zinc binding site 6 out of 6 in 6hc6

Go back to Zinc Binding Sites List in 6hc6
Zinc binding site 6 out of 6 in the The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of The Structure of Bsap, A Zinc Aminopeptidase From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn502

b:21.5
occ:1.00
 NE2 C:HIS401 2.1 17.1 1.0
OD2 C:ASP262 2.1 17.2 1.0
OE1 C:GLU295 2.2 16.9 1.0
OE1 C:GLU452 2.2 18.1 1.0
O C:HOH649 2.3 18.7 1.0
OE2 C:GLU295 2.4 16.4 1.0
CD C:GLU295 2.6 18.7 1.0
CE1 C:HIS401 3.0 18.0 1.0
CG C:ASP262 3.1 14.4 1.0
CD C:GLU452 3.2 23.9 1.0
CD2 C:HIS401 3.2 17.0 1.0
OD1 C:ASP262 3.3 16.0 1.0
OE2 C:GLU452 3.5 23.7 1.0
ZN C:ZN501 3.8 19.2 1.0
O C:HOH851 3.8 18.2 1.0
CE1 C:TYR400 3.8 22.3 1.0
O C:HOH737 4.1 17.6 1.0
OH C:TYR400 4.1 25.6 1.0
ND1 C:HIS401 4.1 21.2 1.0
CG C:GLU295 4.1 15.8 1.0
CG C:HIS401 4.3 17.6 1.0
OE2 C:GLU294 4.3 18.5 1.0
CZ C:TYR400 4.3 26.4 1.0
CB C:ASP262 4.4 14.9 1.0
CG1 C:VAL254 4.5 17.6 1.0
O C:HOH709 4.5 22.1 1.0
CG C:GLU452 4.5 23.1 1.0
CE1 C:HIS250 4.6 16.9 1.0
NE2 C:HIS250 4.7 15.2 1.0
CD1 C:TYR400 4.7 22.3 1.0
CB C:GLU452 4.8 21.8 1.0

Reference:

R.Alhadeff, R.Faygenboim, S.Lansky, E.Rogoulenko, T.Cohen, Y.Fundoiano-Hershcovitz, H.Feinberg, Y.Shoham, G.Shoham. To Be Published To Be Published.
Page generated: Mon Oct 28 22:45:50 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy