Zinc in PDB 1gt7: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli

All present enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli:
4.1.2.19;

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli, PDB code: 1gt7 was solved by M.Kroemer, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.00 / 2.70
Space group	P 32 2 1 1
Cell size a, b, c (Å), α, β, γ (°)	225.760, 225.760, 285.645, 90.00, 90.00, 120.00
R / Rfree (%)	23.3 / 23.5

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20;

Binding sites:

The binding sites of Zinc atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (pdb code 1gt7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 20 binding sites of Zinc where determined in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli, PDB code: 1gt7:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 20 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn275 b:32.3 occ:1.00 NE2 A:HIS212 2.0 36.9 1.0 O2 A:PGH300 2.1 50.4 1.0 NE2 A:HIS141 2.2 28.4 1.0 O1 A:PGH300 2.2 50.2 1.0 NE2 A:HIS143 2.3 26.3 1.0 O A:HOH2177 2.3 37.6 1.0 C1 A:PGH300 2.7 51.1 1.0 N2 A:PGH300 2.8 52.1 1.0 CD2 A:HIS212 3.0 36.5 1.0 CE1 A:HIS212 3.0 36.6 1.0 CE1 A:HIS141 3.1 28.4 1.0 CE1 A:HIS143 3.2 26.5 1.0 CD2 A:HIS141 3.2 29.5 1.0 CD2 A:HIS143 3.3 26.0 1.0 ND1 A:HIS212 4.1 36.0 1.0 C2 A:PGH300 4.1 52.4 1.0 CG A:HIS212 4.2 36.1 1.0 ND1 A:HIS141 4.3 28.9 1.0 N A:GLY31 4.3 31.5 1.0 ND1 A:HIS143 4.3 26.8 1.0 CG A:HIS141 4.3 30.0 1.0 CG A:HIS143 4.4 27.6 1.0 O B:HOH2117 4.5 38.4 1.0 OE1 A:GLU117 4.6 43.3 1.0 CA A:GLY31 4.9 30.0 1.0 O A:HOH2021 4.9 45.3 1.0 O B:HOH2118 4.9 44.1 1.0

Zinc binding site 2 out of 20 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli


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 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn275 b:32.5 occ:1.00 NE2 B:HIS212 2.1 37.0 1.0 NE2 B:HIS141 2.2 28.5 1.0 O1 B:PGH300 2.2 50.2 1.0 O2 B:PGH300 2.2 50.4 1.0 NE2 B:HIS143 2.2 26.4 1.0 O B:HOH2174 2.3 37.5 1.0 C1 B:PGH300 2.7 51.2 1.0 N2 B:PGH300 2.8 52.2 1.0 CD2 B:HIS212 3.0 36.5 1.0 CE1 B:HIS212 3.1 36.6 1.0 CE1 B:HIS143 3.1 26.5 1.0 CE1 B:HIS141 3.1 28.5 1.0 CD2 B:HIS141 3.2 29.4 1.0 CD2 B:HIS143 3.3 26.0 1.0 C2 B:PGH300 4.1 52.4 1.0 ND1 B:HIS212 4.2 36.0 1.0 CG B:HIS212 4.2 36.2 1.0 N B:GLY31 4.2 31.6 1.0 ND1 B:HIS141 4.3 28.9 1.0 ND1 B:HIS143 4.3 26.8 1.0 CG B:HIS141 4.3 29.9 1.0 CG B:HIS143 4.4 27.7 1.0 O C:HOH2118 4.5 38.5 1.0 OE1 B:GLU117 4.7 43.4 1.0 CA B:GLY31 4.8 30.0 1.0 O B:HOH2092 4.9 45.2 1.0 O C:HOH2117 4.9 44.1 1.0

Zinc binding site 3 out of 20 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli


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 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn275 b:32.2 occ:1.00 NE2 C:HIS212 2.1 36.9 1.0 O1 C:PGH300 2.1 50.1 1.0 NE2 C:HIS143 2.2 26.5 1.0 NE2 C:HIS141 2.2 28.6 1.0 O2 C:PGH300 2.2 50.4 1.0 O C:HOH2173 2.4 37.6 1.0 C1 C:PGH300 2.7 51.1 1.0 N2 C:PGH300 2.8 52.2 1.0 CD2 C:HIS212 3.0 36.6 1.0 CE1 C:HIS143 3.1 26.6 1.0 CE1 C:HIS212 3.1 36.7 1.0 CE1 C:HIS141 3.2 28.4 1.0 CD2 C:HIS141 3.2 29.4 1.0 CD2 C:HIS143 3.2 26.0 1.0 C2 C:PGH300 4.1 52.3 1.0 ND1 C:HIS212 4.2 36.0 1.0 CG C:HIS212 4.2 36.1 1.0 ND1 C:HIS143 4.2 26.8 1.0 N C:GLY31 4.2 31.5 1.0 ND1 C:HIS141 4.3 28.9 1.0 CG C:HIS141 4.3 29.9 1.0 CG C:HIS143 4.3 27.6 1.0 O D:HOH2117 4.5 38.5 1.0 OE1 C:GLU117 4.8 43.4 1.0 CA C:GLY31 4.8 29.9 1.0 O D:HOH2116 5.0 44.1 1.0 O C:HOH2093 5.0 45.3 1.0 CA C:GLY30 5.0 30.8 1.0

Zinc binding site 4 out of 20 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli


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 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn275 b:32.3 occ:1.00 NE2 D:HIS212 2.0 36.9 1.0 NE2 D:HIS141 2.1 28.5 1.0 O1 D:PGH300 2.2 50.2 1.0 O2 D:PGH300 2.2 50.5 1.0 NE2 D:HIS143 2.2 26.4 1.0 O D:HOH2173 2.3 37.7 1.0 C1 D:PGH300 2.7 51.1 1.0 N2 D:PGH300 2.8 52.2 1.0 CD2 D:HIS212 3.0 36.5 1.0 CE1 D:HIS212 3.1 36.7 1.0 CE1 D:HIS143 3.1 26.6 1.0 CE1 D:HIS141 3.1 28.5 1.0 CD2 D:HIS141 3.2 29.5 1.0 CD2 D:HIS143 3.2 26.0 1.0 ND1 D:HIS212 4.1 36.1 1.0 C2 D:PGH300 4.2 52.4 1.0 CG D:HIS212 4.2 36.1 1.0 N D:GLY31 4.2 31.5 1.0 ND1 D:HIS141 4.3 28.9 1.0 ND1 D:HIS143 4.3 26.8 1.0 CG D:HIS141 4.3 30.0 1.0 CG D:HIS143 4.4 27.7 1.0 O A:HOH2122 4.6 38.5 1.0 OE1 D:GLU117 4.7 43.4 1.0 CA D:GLY31 4.8 29.9 1.0 O A:HOH2121 4.9 44.0 1.0 CA D:GLY30 5.0 30.7 1.0

Zinc binding site 5 out of 20 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn275 b:33.0 occ:1.00 NE2 E:HIS212 2.0 36.9 1.0 O1 E:PGH300 2.2 50.2 1.0 NE2 E:HIS141 2.2 28.6 1.0 O2 E:PGH300 2.2 50.4 1.0 NE2 E:HIS143 2.2 26.4 1.0 O E:HOH2179 2.4 37.6 1.0 C1 E:PGH300 2.7 51.2 1.0 N2 E:PGH300 2.8 52.2 1.0 CD2 E:HIS212 3.0 36.5 1.0 CE1 E:HIS212 3.1 36.8 1.0 CE1 E:HIS143 3.1 26.7 1.0 CE1 E:HIS141 3.1 28.5 1.0 CD2 E:HIS141 3.2 29.5 1.0 CD2 E:HIS143 3.3 26.1 1.0 C2 E:PGH300 4.1 52.4 1.0 ND1 E:HIS212 4.2 36.0 1.0 CG E:HIS212 4.2 36.2 1.0 N E:GLY31 4.3 31.5 1.0 ND1 E:HIS143 4.3 26.9 1.0 ND1 E:HIS141 4.3 29.0 1.0 CG E:HIS141 4.3 29.9 1.0 CG E:HIS143 4.4 27.8 1.0 O F:HOH2120 4.5 38.7 1.0 OE1 E:GLU117 4.7 43.4 1.0 CA E:GLY31 4.8 30.0 1.0 O E:HOH2100 4.9 45.2 1.0 O F:HOH2119 5.0 44.1 1.0

Zinc binding site 6 out of 20 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn275 b:34.1 occ:1.00 NE2 F:HIS212 2.1 37.0 1.0 O1 F:PGH300 2.1 50.1 1.0 NE2 F:HIS141 2.2 28.5 1.0 O2 F:PGH300 2.2 50.5 1.0 NE2 F:HIS143 2.2 26.6 1.0 O F:HOH2174 2.5 37.9 1.0 C1 F:PGH300 2.7 51.2 1.0 N2 F:PGH300 2.8 52.1 1.0 CD2 F:HIS212 3.1 36.7 1.0 CE1 F:HIS212 3.1 36.8 1.0 CD2 F:HIS141 3.1 29.4 1.0 CE1 F:HIS141 3.1 28.6 1.0 CE1 F:HIS143 3.1 26.8 1.0 CD2 F:HIS143 3.3 26.1 1.0 C2 F:PGH300 4.1 52.4 1.0 N F:GLY31 4.2 31.4 1.0 ND1 F:HIS212 4.2 36.0 1.0 CG F:HIS212 4.2 36.2 1.0 ND1 F:HIS141 4.3 28.9 1.0 CG F:HIS141 4.3 30.0 1.0 ND1 F:HIS143 4.3 26.9 1.0 CG F:HIS143 4.4 27.8 1.0 O G:HOH2120 4.5 38.8 1.0 OE1 F:GLU117 4.7 43.4 1.0 CA F:GLY31 4.8 29.9 1.0 O G:HOH2119 4.9 44.0 1.0

Zinc binding site 7 out of 20 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn275 b:34.1 occ:1.00 NE2 G:HIS212 2.0 36.9 1.0 NE2 G:HIS141 2.1 28.5 1.0 O1 G:PGH300 2.1 50.2 1.0 O2 G:PGH300 2.2 50.4 1.0 NE2 G:HIS143 2.2 26.4 1.0 O G:HOH2176 2.4 37.6 1.0 C1 G:PGH300 2.7 51.1 1.0 N2 G:PGH300 2.8 52.0 1.0 CD2 G:HIS212 3.0 36.6 1.0 CE1 G:HIS212 3.0 36.7 1.0 CE1 G:HIS141 3.1 28.5 1.0 CE1 G:HIS143 3.1 26.6 1.0 CD2 G:HIS141 3.1 29.5 1.0 CD2 G:HIS143 3.2 26.0 1.0 ND1 G:HIS212 4.1 36.0 1.0 CG G:HIS212 4.2 36.1 1.0 C2 G:PGH300 4.2 52.3 1.0 ND1 G:HIS141 4.2 29.0 1.0 N G:GLY31 4.2 31.6 1.0 CG G:HIS141 4.3 29.9 1.0 ND1 G:HIS143 4.3 26.9 1.0 CG G:HIS143 4.4 27.8 1.0 O H:HOH2118 4.5 38.6 1.0 OE1 G:GLU117 4.7 43.4 1.0 CA G:GLY31 4.8 30.0 1.0 O H:HOH2119 4.9 44.1 1.0 O G:HOH2093 5.0 45.3 1.0

Zinc binding site 8 out of 20 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn275 b:32.7 occ:1.00 NE2 H:HIS212 2.1 37.0 1.0 NE2 H:HIS141 2.1 28.4 1.0 O1 H:PGH300 2.1 50.2 1.0 O2 H:PGH300 2.1 50.4 1.0 NE2 H:HIS143 2.2 26.4 1.0 O H:HOH2171 2.4 37.8 1.0 C1 H:PGH300 2.7 51.2 1.0 N2 H:PGH300 2.8 52.1 1.0 CD2 H:HIS212 3.0 36.6 1.0 CE1 H:HIS141 3.1 28.5 1.0 CE1 H:HIS212 3.1 36.6 1.0 CE1 H:HIS143 3.1 26.6 1.0 CD2 H:HIS141 3.1 29.5 1.0 CD2 H:HIS143 3.2 26.1 1.0 ND1 H:HIS212 4.1 35.9 1.0 C2 H:PGH300 4.1 52.4 1.0 CG H:HIS212 4.1 36.1 1.0 ND1 H:HIS141 4.2 28.9 1.0 N H:GLY31 4.3 31.5 1.0 ND1 H:HIS143 4.3 26.7 1.0 CG H:HIS141 4.3 29.9 1.0 CG H:HIS143 4.4 27.6 1.0 O E:HOH2125 4.5 38.4 1.0 OE1 H:GLU117 4.7 43.3 1.0 O E:HOH2124 4.8 44.0 1.0 O H:HOH2012 4.9 45.2 1.0 CA H:GLY31 4.9 29.9 1.0

Zinc binding site 9 out of 20 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ I:Zn275 b:34.5 occ:1.00 NE2 I:HIS212 2.1 37.0 1.0 NE2 I:HIS141 2.1 28.5 1.0 NE2 I:HIS143 2.2 26.5 1.0 O1 I:PGH300 2.2 50.3 1.0 O2 I:PGH300 2.3 50.6 1.0 O I:HOH2177 2.4 37.8 1.0 C1 I:PGH300 2.8 51.2 1.0 N2 I:PGH300 2.9 52.1 1.0 CD2 I:HIS212 3.0 36.6 1.0 CE1 I:HIS143 3.1 26.8 1.0 CE1 I:HIS212 3.1 36.8 1.0 CE1 I:HIS141 3.1 28.7 1.0 CD2 I:HIS141 3.1 29.6 1.0 CD2 I:HIS143 3.2 26.0 1.0 CG I:HIS212 4.2 36.3 1.0 ND1 I:HIS212 4.2 36.1 1.0 N I:GLY31 4.2 31.6 1.0 C2 I:PGH300 4.2 52.5 1.0 ND1 I:HIS143 4.2 27.1 1.0 ND1 I:HIS141 4.3 29.0 1.0 CG I:HIS141 4.3 30.0 1.0 CG I:HIS143 4.3 27.8 1.0 O J:HOH2121 4.5 38.9 1.0 OE1 I:GLU117 4.8 43.4 1.0 CA I:GLY31 4.8 30.0 1.0 O J:HOH2120 5.0 44.2 1.0 CA I:GLY30 5.0 30.9 1.0

Zinc binding site 10 out of 20 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ J:Zn275 b:35.0 occ:1.00 NE2 J:HIS212 2.1 37.1 1.0 NE2 J:HIS143 2.1 26.5 1.0 NE2 J:HIS141 2.2 28.7 1.0 O1 J:PGH300 2.2 50.3 1.0 O2 J:PGH300 2.3 50.5 1.0 O J:HOH2178 2.5 37.7 1.0 C1 J:PGH300 2.8 51.2 1.0 N2 J:PGH300 2.9 52.1 1.0 CD2 J:HIS212 3.0 36.7 1.0 CE1 J:HIS143 3.1 26.7 1.0 CE1 J:HIS141 3.1 28.6 1.0 CE1 J:HIS212 3.1 36.8 1.0 CD2 J:HIS141 3.1 29.6 1.0 CD2 J:HIS143 3.2 26.3 1.0 C2 J:PGH300 4.2 52.4 1.0 N J:GLY31 4.2 31.6 1.0 CG J:HIS212 4.2 36.3 1.0 ND1 J:HIS212 4.2 36.1 1.0 ND1 J:HIS141 4.2 29.0 1.0 ND1 J:HIS143 4.3 27.0 1.0 CG J:HIS141 4.3 30.1 1.0 CG J:HIS143 4.3 27.7 1.0 O K:HOH2122 4.3 38.8 1.0 OE1 J:GLU117 4.7 43.3 1.0 CA J:GLY31 4.8 30.0 1.0 O K:HOH2123 4.8 44.2 1.0 CA J:GLY30 5.0 30.9 1.0

M.Kroemer, G.E.Schulz. The Structure of L-Rhamnulose-1-Phosphate Aldolase (Class II) Solved By Low-Resolution Sir Phasing and 20-Fold Ncs Averaging Acta Crystallogr.,Sect.D V. 58 824 2002.
ISSN: ISSN 0907-4449
PubMed: 11976494
DOI: 10.1107/S0907444902004614