Atomistry » Zinc » PDB 1evr-1f62 » 1ez2
Atomistry »
  Zinc »
    PDB 1evr-1f62 »
      1ez2 »

Zinc in PDB 1ez2: Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.

Enzymatic activity of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.

All present enzymatic activity of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.:
3.1.8.1;

Protein crystallography data

The structure of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate., PDB code: 1ez2 was solved by H.M.Holden, M.M.Benning, F.M.Raushel, S.-B.Hong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 129.400, 91.000, 69.200, 90.00, 91.60, 90.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate. (pdb code 1ez2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate., PDB code: 1ez2:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1ez2

Go back to Zinc Binding Sites List in 1ez2
Zinc binding site 1 out of 4 in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:18.3
occ:1.00
 NE2 A:HIS55 1.7 7.0 1.0
NE2 A:HIS57 2.0 18.7 1.0
O A:HOH1551 2.2 19.2 1.0
OQ2 A:KCX169 2.3 14.5 1.0
OD2 A:ASP301 2.3 13.3 1.0
CE1 A:HIS55 2.8 14.7 1.0
CD2 A:HIS55 2.8 17.2 1.0
CE1 A:HIS57 3.0 25.4 1.0
CX A:KCX169 3.0 14.6 1.0
CD2 A:HIS57 3.1 16.3 1.0
CG A:ASP301 3.1 35.6 1.0
OQ1 A:KCX169 3.2 27.2 1.0
OD1 A:ASP301 3.3 17.8 1.0
ZN A:ZN402 3.3 23.8 1.0
C6 A:DII1403 3.7 24.9 0.7
C4 A:DII1403 3.9 18.7 0.7
ND1 A:HIS55 3.9 10.5 1.0
CG A:HIS55 3.9 9.0 1.0
CE1 A:HIS230 4.0 26.6 1.0
CG2 A:VAL101 4.1 8.3 1.0
ND1 A:HIS57 4.1 21.7 1.0
CG A:HIS57 4.2 21.4 1.0
NE2 A:HIS230 4.2 22.7 1.0
NZ A:KCX169 4.2 19.2 1.0
O1 A:DII1403 4.4 19.9 0.7
CB A:ASP301 4.5 16.6 1.0
C5 A:DII1403 4.7 27.0 0.7
O3 A:DII1403 5.0 34.3 0.7
CA A:ASP301 5.0 11.4 1.0

Zinc binding site 2 out of 4 in 1ez2

Go back to Zinc Binding Sites List in 1ez2
Zinc binding site 2 out of 4 in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:23.8
occ:1.00
 OQ1 A:KCX169 1.8 27.2 1.0
NE2 A:HIS230 2.0 22.7 1.0
O A:HOH1551 2.1 19.2 1.0
ND1 A:HIS201 2.3 27.7 1.0
O1 A:DII1403 2.5 19.9 0.7
CX A:KCX169 2.8 14.6 1.0
CE1 A:HIS230 2.9 26.6 1.0
CD2 A:HIS230 3.1 24.9 1.0
OQ2 A:KCX169 3.2 14.5 1.0
CG A:HIS201 3.2 17.7 1.0
CE1 A:HIS201 3.3 21.1 1.0
ZN A:ZN401 3.3 18.3 1.0
CB A:HIS201 3.4 13.2 1.0
CE1 A:HIS55 3.7 14.7 1.0
NE2 A:HIS55 3.8 7.0 1.0
P1 A:DII1403 3.8 28.4 0.7
ND1 A:HIS230 4.1 26.2 1.0
NE1 A:TRP131 4.1 13.0 1.0
NZ A:KCX169 4.1 19.2 1.0
C7 A:DII1403 4.1 29.6 0.7
CG A:HIS230 4.2 30.1 1.0
OD1 A:ASP301 4.2 17.8 1.0
CD2 A:HIS201 4.3 23.6 1.0
NE2 A:HIS201 4.3 30.1 1.0
CA A:HIS201 4.4 21.1 1.0
C4 A:DII1403 4.4 18.7 0.7
O3 A:DII1403 4.7 34.3 0.7
CD1 A:TRP131 4.7 16.7 1.0
CE A:KCX169 4.8 18.7 1.0
CG A:ASP301 4.9 35.6 1.0
OD2 A:ASP301 4.9 13.3 1.0
ND1 A:HIS55 5.0 10.5 1.0

Zinc binding site 3 out of 4 in 1ez2

Go back to Zinc Binding Sites List in 1ez2
Zinc binding site 3 out of 4 in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:16.8
occ:1.00
 NE2 B:HIS55 1.8 6.0 1.0
NE2 B:HIS57 2.1 19.4 1.0
O B:HOH2609 2.1 13.6 1.0
OQ1 B:KCX169 2.2 16.2 1.0
OD2 B:ASP301 2.3 13.4 1.0
CE1 B:HIS55 2.8 6.4 1.0
CD2 B:HIS55 2.9 12.5 1.0
CE1 B:HIS57 3.0 16.1 1.0
CX B:KCX169 3.1 15.4 1.0
CD2 B:HIS57 3.1 11.7 1.0
CG B:ASP301 3.1 27.4 1.0
OD1 B:ASP301 3.3 19.6 1.0
ZN B:ZN402 3.3 19.2 1.0
OQ2 B:KCX169 3.4 23.4 1.0
C1 B:DII2403 3.9 37.7 0.7
ND1 B:HIS55 3.9 7.9 1.0
CG B:HIS55 4.0 9.1 1.0
CG2 B:VAL101 4.0 13.3 1.0
CE1 B:HIS230 4.1 18.6 1.0
ND1 B:HIS57 4.2 15.3 1.0
CG B:HIS57 4.2 19.4 1.0
NE2 B:HIS230 4.2 17.0 1.0
C3 B:DII2403 4.2 32.5 0.7
C2 B:DII2403 4.3 25.4 0.7
NZ B:KCX169 4.4 23.9 1.0
CB B:ASP301 4.4 14.3 1.0
O1 B:DII2403 4.4 21.8 0.7
C7 B:DII2403 4.9 22.4 0.7
O2 B:DII2403 4.9 65.8 0.7
CA B:ASP301 5.0 11.6 1.0

Zinc binding site 4 out of 4 in 1ez2

Go back to Zinc Binding Sites List in 1ez2
Zinc binding site 4 out of 4 in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Diisopropylmethyl Phosphonate. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn402

b:19.2
occ:1.00
 O B:HOH2609 2.0 13.6 1.0
NE2 B:HIS230 2.0 17.0 1.0
ND1 B:HIS201 2.0 20.0 1.0
OQ2 B:KCX169 2.1 23.4 1.0
O1 B:DII2403 2.6 21.8 0.7
CE1 B:HIS201 2.9 20.1 1.0
CX B:KCX169 3.0 15.4 1.0
CE1 B:HIS230 3.0 18.6 1.0
CD2 B:HIS230 3.1 21.0 1.0
CG B:HIS201 3.1 18.3 1.0
OQ1 B:KCX169 3.3 16.2 1.0
ZN B:ZN401 3.3 16.8 1.0
CB B:HIS201 3.5 7.5 1.0
P1 B:DII2403 3.7 28.9 0.7
CE1 B:HIS55 3.8 6.4 1.0
C7 B:DII2403 3.8 22.4 0.7
NE2 B:HIS55 4.0 6.0 1.0
NE2 B:HIS201 4.1 19.9 1.0
OD1 B:ASP301 4.1 19.6 1.0
ND1 B:HIS230 4.2 15.2 1.0
NE1 B:TRP131 4.2 15.6 1.0
CG B:HIS230 4.2 28.3 1.0
CD2 B:HIS201 4.2 16.2 1.0
NZ B:KCX169 4.3 23.9 1.0
CA B:HIS201 4.4 17.8 1.0
C1 B:DII2403 4.5 37.7 0.7
O2 B:DII2403 4.6 65.8 0.7
CE B:KCX169 4.6 18.6 1.0
CD1 B:TRP131 4.8 17.1 1.0
CG B:ASP301 4.8 27.4 1.0
OD2 B:ASP301 4.8 13.4 1.0
O3 B:DII2403 4.9 51.1 0.7

Reference:

M.M.Benning, S.B.Hong, F.M.Raushel, H.M.Holden. The Binding of Substrate Analogs to Phosphotriesterase. J.Biol.Chem. V. 275 30556 2000.
ISSN: ISSN 0021-9258
PubMed: 10871616
DOI: 10.1074/JBC.M003852200
Page generated: Tue Aug 19 20:01:40 2025

Last articles

K in 9NES
K in 9PHG
K in 9NEI
K in 9NED
K in 9NEC
K in 9NEG
K in 9CWU
K in 9CVB
K in 9CVA
K in 9COM
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy