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Mercury in PDB 1arm: Carboxypeptidase A with Zn Replaced By Hg

Enzymatic activity of Carboxypeptidase A with Zn Replaced By Hg

All present enzymatic activity of Carboxypeptidase A with Zn Replaced By Hg:
3.4.17.1;

Protein crystallography data

The structure of Carboxypeptidase A with Zn Replaced By Hg, PDB code: 1arm was solved by H.M.Greenblatt, H.Feinberg, P.A.Tucker, G.Shoham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.10 / 1.76
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.700, 60.320, 47.200, 90.00, 97.39, 90.00
R / Rfree (%) 14.6 / n/a

Other elements in 1arm:

The structure of Carboxypeptidase A with Zn Replaced By Hg also contains other interesting chemical elements:

Copper (Cu) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Carboxypeptidase A with Zn Replaced By Hg (pdb code 1arm). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the Carboxypeptidase A with Zn Replaced By Hg, PDB code: 1arm:
Jump to Mercury binding site number: 1; 2; 3; 4;

Mercury binding site 1 out of 4 in 1arm

Go back to Mercury Binding Sites List in 1arm
Mercury binding site 1 out of 4 in the Carboxypeptidase A with Zn Replaced By Hg


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Carboxypeptidase A with Zn Replaced By Hg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg310

b:17.4
occ:1.00
ND1 A:HIS196 2.1 10.7 1.0
ND1 A:HIS69 2.3 10.2 1.0
N A:TRS319 2.4 1.1 0.4
O A:HOH320 2.5 10.2 0.6
OE1 A:GLU72 2.5 8.9 1.0
OE2 A:GLU72 2.6 14.6 1.0
O2 A:TRS319 2.8 9.1 0.4
CD A:GLU72 2.9 10.5 1.0
CE1 A:HIS196 3.1 11.0 1.0
CG A:HIS196 3.2 11.5 1.0
CE1 A:HIS69 3.2 16.1 1.0
C A:TRS319 3.3 6.7 0.4
CG A:HIS69 3.3 12.5 1.0
C1 A:TRS319 3.3 13.5 0.4
CB A:HIS196 3.5 6.2 1.0
CB A:HIS69 3.6 14.4 1.0
C2 A:TRS319 3.6 13.1 0.4
O A:SER197 3.9 16.0 1.0
O1 A:TRS319 4.3 66.3 0.4
NE2 A:HIS196 4.4 15.5 1.0
CD2 A:HIS196 4.4 16.9 1.0
NE2 A:HIS69 4.4 19.6 1.0
CG A:GLU72 4.4 11.4 1.0
CD2 A:HIS69 4.5 12.7 1.0
CA A:HIS196 4.5 16.1 1.0
OE2 A:GLU270 4.5 24.5 1.0
N A:SER197 4.5 11.9 1.0
O A:HOH321 4.6 12.2 0.4
O A:HOH334 4.6 14.4 1.0
O A:HOH427 4.7 38.6 0.5
C3 A:TRS319 4.7 10.0 0.4
OE1 A:GLU270 4.7 23.3 1.0
NH1 A:ARG127 4.9 72.9 1.0
C A:SER197 5.0 12.3 1.0
CA A:HIS69 5.0 5.9 1.0
CD A:GLU270 5.0 34.6 1.0

Mercury binding site 2 out of 4 in 1arm

Go back to Mercury Binding Sites List in 1arm
Mercury binding site 2 out of 4 in the Carboxypeptidase A with Zn Replaced By Hg


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Carboxypeptidase A with Zn Replaced By Hg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg316

b:24.8
occ:0.40
NZ A:LYS84 2.3 24.1 1.0
NE2 A:HIS29 2.3 34.7 1.0
CE1 A:HIS29 2.8 20.4 1.0
CE A:LYS84 3.2 27.7 1.0
OE1 A:GLU28 3.3 39.2 1.0
OG1 A:THR87 3.4 19.1 1.0
CD2 A:HIS29 3.5 32.3 1.0
CD A:LYS84 3.5 23.3 1.0
OE2 A:GLU88 3.5 0.0 1.0
OG1 A:THR4 3.6 26.4 1.0
ND1 A:HIS29 4.1 30.4 1.0
CG A:HIS29 4.4 14.7 1.0
CB A:THR87 4.4 14.7 1.0
CD1 A:LEU25 4.4 22.9 1.0
CD A:GLU28 4.6 38.2 1.0
ND2 A:ASN5 4.7 28.5 1.0
CD A:GLU88 4.8 0.0 1.0
CB A:GLU28 4.9 18.4 1.0
CB A:THR4 4.9 13.7 1.0
OD1 A:ASN5 5.0 51.5 1.0

Mercury binding site 3 out of 4 in 1arm

Go back to Mercury Binding Sites List in 1arm
Mercury binding site 3 out of 4 in the Carboxypeptidase A with Zn Replaced By Hg


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Carboxypeptidase A with Zn Replaced By Hg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg317

b:32.7
occ:0.40
O A:HOH376 2.4 24.0 0.9
O A:HOH446 2.9 84.6 0.8
O A:HOH428 3.2 40.9 0.8
O A:HOH417 3.9 34.3 0.9
O A:HOH487 4.1 47.6 1.0
NE1 A:TRP81 4.4 17.7 1.0
CZ2 A:TRP81 4.8 18.0 1.0
CE2 A:TRP81 5.0 10.3 1.0

Mercury binding site 4 out of 4 in 1arm

Go back to Mercury Binding Sites List in 1arm
Mercury binding site 4 out of 4 in the Carboxypeptidase A with Zn Replaced By Hg


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Carboxypeptidase A with Zn Replaced By Hg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg318

b:34.8
occ:0.40
ND1 A:HIS29 2.3 30.4 1.0
CG A:HIS29 3.1 14.7 1.0
O A:HOH481 3.1 37.9 0.7
O A:HOH499 3.2 35.7 1.0
CB A:HIS29 3.2 13.9 1.0
CE1 A:HIS29 3.4 20.4 1.0
CA A:HIS29 3.8 20.0 1.0
O A:GLU28 4.1 27.2 1.0
CD2 A:HIS29 4.3 32.3 1.0
NE2 A:HIS29 4.4 34.7 1.0
C A:HIS29 4.7 24.0 1.0
N A:HIS29 4.8 17.2 1.0
CD2 A:LEU32 4.8 37.9 1.0
CB A:LEU32 4.9 22.4 1.0
C A:GLU28 4.9 27.5 1.0
O A:THR87 5.0 23.3 1.0
O A:HIS29 5.0 26.6 1.0

Reference:

H.M.Greenblatt, H.Feinberg, P.A.Tucker, G.Shoham. Carboxypeptidase A: Native, Zinc-Removed and Mercury-Replaced Forms. Acta Crystallogr.,Sect.D V. 54 289 1998.
ISSN: ISSN 0907-4449
PubMed: 9867434
DOI: 10.1107/S0907444997010445
Page generated: Wed Oct 28 18:38:47 2020

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