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Zinc in PDB 2qfr: Crystal Structure of Red Kidney Bean Purple Acid Phosphatase with Bound Sulfate

Enzymatic activity of Crystal Structure of Red Kidney Bean Purple Acid Phosphatase with Bound Sulfate

All present enzymatic activity of Crystal Structure of Red Kidney Bean Purple Acid Phosphatase with Bound Sulfate:
3.1.3.2;

Protein crystallography data

The structure of Crystal Structure of Red Kidney Bean Purple Acid Phosphatase with Bound Sulfate, PDB code: 2qfr was solved by L.W.Guddat, G.Schenk, L.R.Gahan, T.W.Elliot, E.Leung, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.00 / 2.40
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 148.030, 148.030, 160.090, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 21.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Red Kidney Bean Purple Acid Phosphatase with Bound Sulfate (pdb code 2qfr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Red Kidney Bean Purple Acid Phosphatase with Bound Sulfate, PDB code: 2qfr:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2qfr

Go back to Zinc Binding Sites List in 2qfr
Zinc binding site 1 out of 2 in the Crystal Structure of Red Kidney Bean Purple Acid Phosphatase with Bound Sulfate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Red Kidney Bean Purple Acid Phosphatase with Bound Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn434

b:16.8
occ:1.00
OD1 A:ASN201 2.0 25.2 1.0
NE2 A:HIS286 2.0 15.7 1.0
ND1 A:HIS323 2.1 18.7 1.0
OD2 A:ASP164 2.4 21.4 1.0
O A:HOH454 2.4 29.2 1.0
CE1 A:HIS286 2.9 15.7 1.0
CE1 A:HIS323 2.9 18.7 1.0
FE A:FE433 3.1 22.2 1.0
CG A:ASN201 3.1 21.1 1.0
CD2 A:HIS286 3.1 14.8 1.0
CG A:HIS323 3.2 18.5 1.0
CA A:HIS323 3.3 15.7 1.0
CG A:ASP164 3.3 20.5 1.0
OD1 A:ASP164 3.6 19.0 1.0
OD2 A:ASP135 3.6 20.9 1.0
CB A:HIS323 3.6 16.6 1.0
ND2 A:ASN201 3.7 20.6 1.0
O3 A:SO4435 3.7 73.4 1.0
O A:HIS323 3.8 19.5 1.0
C A:HIS323 4.1 17.3 1.0
ND1 A:HIS286 4.1 14.9 1.0
NE2 A:HIS323 4.1 19.3 1.0
N A:HIS323 4.2 14.2 1.0
CG A:HIS286 4.2 15.8 1.0
CD2 A:HIS323 4.2 17.4 1.0
CB A:ASN201 4.3 18.0 1.0
N A:ASN201 4.4 14.8 1.0
CD2 A:HIS202 4.5 22.8 1.0
CB A:ASP164 4.6 19.6 1.0
CG A:ASP135 4.8 19.5 1.0
O1 A:SO4435 4.8 72.9 1.0
NE2 A:HIS325 4.8 26.0 1.0
OH A:TYR167 4.8 18.4 1.0
S A:SO4435 4.9 73.0 1.0
OH A:TYR253 4.9 12.4 1.0
CA A:ASN201 4.9 14.9 1.0

Zinc binding site 2 out of 2 in 2qfr

Go back to Zinc Binding Sites List in 2qfr
Zinc binding site 2 out of 2 in the Crystal Structure of Red Kidney Bean Purple Acid Phosphatase with Bound Sulfate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Red Kidney Bean Purple Acid Phosphatase with Bound Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn434

b:20.4
occ:1.00
NE2 B:HIS286 2.0 16.4 1.0
ND1 B:HIS323 2.1 15.7 1.0
OD1 B:ASN201 2.1 22.4 1.0
OD2 B:ASP164 2.2 22.4 1.0
O B:HOH454 2.3 26.8 1.0
CE1 B:HIS323 2.9 15.3 1.0
CE1 B:HIS286 2.9 15.7 1.0
CD2 B:HIS286 3.1 15.2 1.0
FE B:FE433 3.1 27.5 1.0
CG B:HIS323 3.2 16.4 1.0
CG B:ASP164 3.2 20.2 1.0
CG B:ASN201 3.3 20.7 1.0
CA B:HIS323 3.3 15.3 1.0
OD1 B:ASP164 3.5 18.4 1.0
OD2 B:ASP135 3.5 24.2 1.0
CB B:HIS323 3.6 13.9 1.0
O2 B:SO4435 3.6 70.5 1.0
ND2 B:ASN201 3.9 20.7 1.0
O B:HIS323 3.9 16.6 1.0
ND1 B:HIS286 4.1 16.1 1.0
NE2 B:HIS323 4.1 17.7 1.0
C B:HIS323 4.1 16.8 1.0
CG B:HIS286 4.2 16.6 1.0
N B:HIS323 4.2 14.8 1.0
CD2 B:HIS323 4.2 16.1 1.0
CB B:ASN201 4.4 18.4 1.0
N B:ASN201 4.4 16.7 1.0
CD2 B:HIS202 4.5 22.1 1.0
CB B:ASP164 4.5 21.0 1.0
O4 B:SO4435 4.6 71.8 1.0
CG B:ASP135 4.7 21.5 1.0
S B:SO4435 4.8 71.5 1.0
OH B:TYR167 4.8 13.1 1.0
NE2 B:HIS325 4.9 24.6 1.0
OH B:TYR253 5.0 11.9 1.0
CA B:ASN201 5.0 16.7 1.0

Reference:

G.Schenk, T.W.Elliott, E.Leung, L.E.Carrington, N.Mitic, L.R.Gahan, L.W.Guddat. Crystal Structures of A Purple Acid Phosphatase, Representing Different Steps of This Enzyme'S Catalytic Cycle. Bmc Struct.Biol. V. 8 6 2008.
ISSN: ESSN 1472-6807
PubMed: 18234116
DOI: 10.1186/1472-6807-8-6
Page generated: Sat Sep 26 03:41:19 2020
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