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Zinc in PDB 2uyv: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A)

Enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A)

All present enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A):
4.1.2.19;

Protein crystallography data

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A), PDB code: 2uyv was solved by D.Grueninger, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 95.565, 102.355, 265.500, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 24.4

Zinc Binding Sites:

The binding sites of Zinc atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A) (pdb code 2uyv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A), PDB code: 2uyv:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2uyv

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Zinc binding site 1 out of 4 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1276

b:32.5
occ:1.00
O A:HOH2253 2.1 54.0 1.0
NE2 A:HIS212 2.2 30.8 1.0
NE2 A:HIS141 2.2 25.4 1.0
NE2 A:HIS143 2.3 23.3 1.0
O4 A:TLA1277 2.7 75.0 1.0
CD2 A:HIS212 3.1 29.5 1.0
CD2 A:HIS141 3.1 26.0 1.0
CE1 A:HIS212 3.2 30.9 1.0
CE1 A:HIS141 3.2 26.5 1.0
CD2 A:HIS143 3.2 27.1 1.0
O3 A:TLA1277 3.3 74.3 1.0
CE1 A:HIS143 3.3 26.0 1.0
C4 A:TLA1277 3.4 75.4 1.0
O4 A:TLA1275 3.6 66.7 1.0
C3 A:TLA1277 3.8 75.3 1.0
O41 A:TLA1275 3.9 65.2 1.0
N A:GLY31 4.1 30.8 1.0
O41 A:TLA1277 4.2 77.0 1.0
CG A:HIS212 4.2 31.2 1.0
C4 A:TLA1275 4.2 65.2 1.0
ND1 A:HIS212 4.3 31.6 1.0
CG A:HIS141 4.3 27.6 1.0
ND1 A:HIS141 4.3 27.0 1.0
CG A:HIS143 4.4 26.4 1.0
ND1 A:HIS143 4.4 28.8 1.0
OE1 A:GLU117 4.5 55.1 1.0
CA A:GLY31 4.7 31.5 1.0
O B:HOH2179 4.8 42.6 1.0
CA A:GLY30 4.9 29.7 1.0
CZ3 A:TRP209 4.9 36.5 1.0
C A:GLY30 4.9 30.7 1.0

Zinc binding site 2 out of 4 in 2uyv

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Zinc binding site 2 out of 4 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1276

b:34.0
occ:1.00
O1 B:TLA1275 2.1 52.8 0.5
NE2 B:HIS212 2.2 33.8 1.0
NE2 B:HIS141 2.2 29.5 1.0
NE2 B:HIS143 2.2 17.6 1.0
O1 B:TLA1275 2.3 29.9 0.5
O11 B:TLA1275 2.3 31.9 0.5
C1 B:TLA1275 2.6 32.4 0.5
C1 B:TLA1275 2.7 53.5 0.5
O11 B:TLA1275 2.8 52.7 0.5
CD2 B:HIS212 3.1 32.9 1.0
CD2 B:HIS141 3.1 28.8 1.0
CD2 B:HIS143 3.2 20.4 1.0
CE1 B:HIS212 3.2 32.9 1.0
CE1 B:HIS141 3.2 28.8 1.0
CE1 B:HIS143 3.3 19.9 1.0
OE1 C:GLU171 3.9 44.0 1.0
C2 B:TLA1275 4.0 32.9 0.5
C2 B:TLA1275 4.1 53.5 0.5
N B:GLY31 4.2 29.9 1.0
CG B:HIS212 4.2 33.7 1.0
ND1 B:HIS212 4.3 33.3 1.0
CG B:HIS141 4.3 29.5 1.0
ND1 B:HIS141 4.3 30.3 1.0
O B:HOH2264 4.3 33.6 0.5
O3 B:TLA1275 4.3 35.2 0.5
CD C:GLU171 4.3 40.5 1.0
CG B:HIS143 4.4 21.4 1.0
ND1 B:HIS143 4.4 20.8 1.0
OE2 C:GLU171 4.4 43.1 1.0
C3 B:TLA1275 4.6 35.1 0.5
O2 B:TLA1275 4.7 30.2 0.5
C3 B:TLA1275 4.8 53.1 0.5
O B:HOH2260 4.8 70.5 1.0
CA B:GLY31 4.8 30.8 1.0
CZ3 B:TRP209 4.9 38.2 1.0
CA B:GLY30 5.0 29.8 1.0
O3 B:TLA1275 5.0 53.4 0.5

Zinc binding site 3 out of 4 in 2uyv

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Zinc binding site 3 out of 4 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1276

b:31.5
occ:1.00
NE2 C:HIS212 2.1 31.6 1.0
O1 C:TLA1275 2.2 41.1 1.0
NE2 C:HIS141 2.2 29.0 1.0
NE2 C:HIS143 2.3 25.5 1.0
O11 C:TLA1275 2.5 38.7 1.0
C1 C:TLA1275 2.6 42.4 1.0
CD2 C:HIS212 3.0 32.0 1.0
CD2 C:HIS141 3.2 28.9 1.0
CE1 C:HIS212 3.2 32.0 1.0
CD2 C:HIS143 3.2 26.4 1.0
CE1 C:HIS141 3.2 29.2 1.0
CE1 C:HIS143 3.3 28.6 1.0
OE1 D:GLU171 3.7 53.0 1.0
CD D:GLU171 4.1 50.5 1.0
C2 C:TLA1275 4.1 43.1 1.0
N C:GLY31 4.2 30.8 1.0
CG C:HIS212 4.2 31.8 1.0
ND1 C:HIS212 4.2 32.9 1.0
OE2 D:GLU171 4.2 53.1 1.0
CG C:HIS141 4.3 30.2 1.0
ND1 C:HIS141 4.3 29.9 1.0
CG C:HIS143 4.4 26.6 1.0
ND1 C:HIS143 4.4 29.1 1.0
O3 C:TLA1275 4.6 44.9 1.0
O2 C:TLA1275 4.7 42.8 1.0
C3 C:TLA1275 4.8 44.7 1.0
CA C:GLY31 4.8 28.2 1.0
CZ3 C:TRP209 4.9 37.0 1.0
O D:HOH2157 4.9 43.2 1.0
CA C:GLY30 4.9 30.8 1.0

Zinc binding site 4 out of 4 in 2uyv

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Zinc binding site 4 out of 4 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1276

b:38.5
occ:1.00
NE2 D:HIS141 2.2 28.2 1.0
NE2 D:HIS212 2.3 31.5 1.0
O11 D:TLA1275 2.3 44.5 1.0
NE2 D:HIS143 2.4 28.7 1.0
O D:HOH2224 2.4 53.3 1.0
O D:HOH2222 2.8 58.3 1.0
O1 D:TLA1275 3.0 53.7 1.0
C1 D:TLA1275 3.0 51.7 1.0
CD2 D:HIS141 3.1 27.4 1.0
CD2 D:HIS212 3.2 32.6 1.0
CE1 D:HIS212 3.3 30.1 1.0
CE1 D:HIS141 3.3 27.9 1.0
CD2 D:HIS143 3.4 29.6 1.0
CE1 D:HIS143 3.4 28.0 1.0
N D:GLY31 3.9 32.4 1.0
CG D:HIS141 4.3 29.9 1.0
ND1 D:HIS141 4.4 28.2 1.0
ND1 D:HIS212 4.4 33.0 1.0
CG D:HIS212 4.4 31.3 1.0
C2 D:TLA1275 4.5 53.6 1.0
ND1 D:HIS143 4.5 29.5 1.0
CA D:GLY31 4.5 30.2 1.0
CG D:HIS143 4.5 27.7 1.0
CA D:GLY30 4.9 33.5 1.0
C D:GLY30 4.9 33.9 1.0
ND2 D:ASN32 4.9 35.9 1.0
O2 D:TLA1275 4.9 55.5 1.0
O A:HOH2188 4.9 65.9 1.0
OE1 D:GLU117 5.0 43.2 1.0
CZ3 D:TRP209 5.0 37.1 1.0

Reference:

D.Grueninger, N.Treiber, M.O.P.Ziegler, J.W.A.Koetter, M.-S.Schulze, G.E.Schulz. Designed Protein-Protein Association. Science V. 319 206 2008.
ISSN: ISSN 0036-8075
PubMed: 18187656
DOI: 10.1126/SCIENCE.1150421
Page generated: Sat Sep 26 03:57:56 2020
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