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Zinc in PDB 8r75: Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 1

Protein crystallography data

The structure of Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 1, PDB code: 8r75 was solved by A.Cartmell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.51 / 2.70
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 74.37, 101.58, 161.83, 90, 90, 90
R / Rfree (%) 18 / 27.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 1 (pdb code 8r75). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 1, PDB code: 8r75:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 8r75

Go back to Zinc Binding Sites List in 8r75
Zinc binding site 1 out of 2 in the Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:101.7
occ:1.00
HD1 A:HIS446 1.3 30.0 0.0
HE2 A:HIS490 1.3 30.0 0.0
OD1 A:ASP464 1.9 80.9 1.0
ND1 A:HIS446 2.0 86.9 1.0
NE2 A:HIS490 2.1 88.9 1.0
HE1 A:HIS446 2.5 86.5 1.0
CE1 A:HIS446 2.6 87.2 1.0
CG A:ASP464 2.9 82.0 1.0
CE1 A:HIS490 3.1 99.9 1.0
CD2 A:HIS490 3.2 88.5 1.0
CG A:HIS446 3.2 88.3 1.0
HE1 A:HIS490 3.3 91.2 1.0
HD2 A:HIS490 3.4 85.3 1.0
OD2 A:ASP464 3.4 91.0 1.0
H A:ALA343 3.5 100.6 1.0
H A:GLY466 3.6 86.5 1.0
O A:ALA343 3.7 95.6 1.0
HB2 A:HIS446 3.7 90.6 1.0
HB3 A:HIS446 3.8 91.9 1.0
NE2 A:HIS446 3.8 84.2 1.0
CB A:HIS446 3.9 91.2 1.0
HA2 A:GLY466 4.0 84.8 1.0
N A:ALA343 4.1 97.2 1.0
CD2 A:HIS446 4.2 90.5 1.0
CB A:ASP464 4.2 83.2 1.0
HA A:ALA343 4.2 106.7 1.0
O A:THR484 4.2 93.1 1.0
ND1 A:HIS490 4.2 76.3 1.0
O A:ASN341 4.2 96.3 1.0
OD2 A:ASP448 4.3 78.9 1.0
HB3 A:ASP464 4.3 81.8 1.0
CG A:HIS490 4.3 77.8 1.0
H A:ALA465 4.3 82.9 1.0
N A:GLY466 4.3 86.5 1.0
C A:ALA343 4.4 109.7 1.0
HB3 A:ASP448 4.4 99.1 1.0
HA A:PHE342 4.4 97.0 1.0
CA A:ALA343 4.5 111.5 1.0
HA A:ASP464 4.6 82.1 1.0
N A:ALA465 4.6 82.5 1.0
CA A:GLY466 4.7 81.8 1.0
HE2 A:HIS446 4.7 30.0 0.0
CA A:ASP464 4.8 81.5 1.0
C A:ASP464 4.8 81.5 1.0
HB2 A:ASP464 4.9 82.2 1.0
C A:PHE342 5.0 96.5 1.0

Zinc binding site 2 out of 2 in 8r75

Go back to Zinc Binding Sites List in 8r75
Zinc binding site 2 out of 2 in the Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn701

b:96.2
occ:1.00
HD1 B:HIS446 1.5 30.0 0.0
HE2 B:HIS490 1.6 30.0 0.0
OD1 B:ASP464 2.1 89.3 1.0
ND1 B:HIS446 2.2 100.5 1.0
NE2 B:HIS490 2.4 56.8 1.0
HE1 B:HIS446 2.5 97.8 1.0
CE1 B:HIS446 2.6 105.2 1.0
CG B:ASP464 2.8 75.5 1.0
OD2 B:ASP464 3.2 93.6 1.0
CE1 B:HIS490 3.3 61.6 1.0
CD2 B:HIS490 3.4 79.6 1.0
H B:ALA343 3.4 84.0 1.0
CG B:HIS446 3.5 84.0 1.0
HD2 B:HIS490 3.5 70.0 1.0
HE1 B:HIS490 3.5 60.1 1.0
O B:ALA343 3.6 120.4 1.0
H B:GLY466 3.6 79.7 1.0
NE2 B:HIS446 3.9 82.3 1.0
HB2 B:HIS446 3.9 83.5 1.0
N B:ALA343 4.0 81.7 1.0
HB3 B:ASP464 4.0 70.2 1.0
CB B:ASP464 4.0 67.2 1.0
O B:ASN341 4.0 79.7 1.0
HA2 B:GLY466 4.0 77.6 1.0
CB B:HIS446 4.2 85.8 1.0
HB3 B:HIS446 4.2 83.8 1.0
HA B:PHE342 4.2 80.6 1.0
HA B:ALA343 4.3 93.3 1.0
C B:ALA343 4.3 106.8 1.0
CD2 B:HIS446 4.3 94.0 1.0
H B:ALA465 4.3 72.6 1.0
N B:GLY466 4.3 82.2 1.0
O B:THR484 4.4 80.4 1.0
CA B:ALA343 4.4 94.5 1.0
ND1 B:HIS490 4.5 58.2 1.0
CG B:HIS490 4.5 65.4 1.0
HA B:ASP464 4.6 73.2 1.0
OD2 B:ASP448 4.6 96.5 1.0
N B:ALA465 4.6 71.0 1.0
CA B:GLY466 4.6 79.7 1.0
CA B:ASP464 4.7 73.4 1.0
HE2 B:HIS446 4.7 30.0 0.0
HB3 B:ASP448 4.7 71.2 1.0
HB2 B:ASP464 4.7 70.4 1.0
C B:ASP464 4.8 80.9 1.0
C B:PHE342 4.8 79.4 1.0
CA B:PHE342 5.0 85.6 1.0

Reference:

A.Cartmell, M.Couturier. Polysaccharide Lyase Family 33 Utilises An Evolutionary Conserved Mechanism of Conformationally Induced Catalysis to Drive Processivity To Be Published.
Page generated: Tue Dec 10 21:50:58 2024

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