Zinc in PDB 1uqw: Crystal Structure of Ylib Protein From Escherichia Coi

The structure of Crystal Structure of Ylib Protein From Escherichia Coi, PDB code: 1uqw was solved by S.Jeudy, C.Abergel, J.M.Claverie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 2.72
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	152.560, 82.540, 93.300, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 25.6

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Zinc atom in the Crystal Structure of Ylib Protein From Escherichia Coi (pdb code 1uqw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 12 binding sites of Zinc where determined in the Crystal Structure of Ylib Protein From Escherichia Coi, PDB code: 1uqw:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 12 in the Crystal Structure of Ylib Protein From Escherichia Coi


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 Ylib Protein From Escherichia Coi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:78.4 occ:1.00 O A:HIS99 2.4 29.8 1.0 ND1 A:HIS99 2.5 46.1 1.0 CE1 A:HIS99 3.1 46.0 1.0 C A:HIS99 3.6 31.4 1.0 CG A:HIS99 3.7 43.1 1.0 OD2 A:ASP22 4.0 26.1 1.0 CB A:HIS99 4.3 37.3 1.0 OD1 A:ASP22 4.3 29.0 1.0 O A:ASN98 4.3 28.1 1.0 NE2 A:HIS99 4.4 45.5 1.0 N A:LEU100 4.5 29.3 1.0 CA A:HIS99 4.6 33.4 1.0 CG A:ASP22 4.6 26.6 1.0 CA A:LEU100 4.6 26.4 1.0 CD2 A:HIS99 4.7 44.4 1.0 N A:LYS101 4.9 23.7 1.0

Zinc binding site 2 out of 12 in the Crystal Structure of Ylib Protein From Escherichia Coi


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 Ylib Protein From Escherichia Coi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:48.0 occ:1.00 OE1 A:GLU149 2.3 42.8 1.0 ZN A:ZN502 2.9 54.0 1.0 O A:HOH2146 3.0 33.5 1.0 CD A:GLU149 3.3 41.7 1.0 OE2 A:GLU149 3.6 44.7 1.0 CG A:GLU149 4.5 37.5 1.0

Zinc binding site 3 out of 12 in the Crystal Structure of Ylib Protein From Escherichia Coi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Ylib Protein From Escherichia Coi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:54.0 occ:1.00 OE2 A:GLU149 2.2 44.7 1.0 ZN A:ZN501 2.9 48.0 1.0 CD A:GLU149 3.0 41.7 1.0 OE1 A:GLU149 3.2 42.8 1.0 CG A:GLU149 4.4 37.5 1.0

Zinc binding site 4 out of 12 in the Crystal Structure of Ylib Protein From Escherichia Coi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Ylib Protein From Escherichia Coi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn503 b:45.4 occ:1.00 OD1 A:ASP168 2.5 29.2 1.0 O A:HOH2147 2.8 29.5 1.0 O A:HOH2149 3.0 15.3 1.0 ZN A:ZN504 3.0 43.7 1.0 OD2 A:ASP168 3.2 27.0 1.0 CG A:ASP168 3.2 26.5 1.0 NZ A:LYS177 4.1 27.3 1.0 CG2 A:THR169 4.2 28.7 1.0 CD A:LYS177 4.2 26.2 1.0 CE A:LYS177 4.4 26.1 1.0 O A:HOH2069 4.6 20.5 1.0 CB A:ASP168 4.7 26.0 1.0

Zinc binding site 5 out of 12 in the Crystal Structure of Ylib Protein From Escherichia Coi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Ylib Protein From Escherichia Coi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn504 b:43.7 occ:1.00 O A:HOH2148 2.4 13.8 1.0 OD2 A:ASP168 2.7 27.0 1.0 O A:HOH2149 2.9 15.3 1.0 ZN A:ZN503 3.0 45.4 1.0 CG A:ASP168 3.5 26.5 1.0 OD1 A:ASP168 3.7 29.2 1.0 O A:HOH2069 4.2 20.5 1.0 NZ A:LYS179 4.7 27.1 1.0 CB A:ASP168 4.8 26.0 1.0 CD A:LYS179 5.0 23.6 1.0

Zinc binding site 6 out of 12 in the Crystal Structure of Ylib Protein From Escherichia Coi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of Ylib Protein From Escherichia Coi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn505 b:42.3 occ:1.00 OE2 A:GLU214 2.3 24.4 1.0 O A:HOH2150 2.4 27.6 1.0 OE1 A:GLU214 2.7 19.8 1.0 CD A:GLU214 2.8 20.9 1.0 NH2 A:ARG198 4.0 28.7 1.0 CG A:GLU214 4.3 17.6 1.0 NH1 A:ARG198 4.7 29.0 1.0 CZ A:ARG198 4.9 28.7 1.0

Zinc binding site 7 out of 12 in the Crystal Structure of Ylib Protein From Escherichia Coi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of Ylib Protein From Escherichia Coi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn506 b:67.7 occ:1.00 NE2 A:HIS466 2.2 28.6 1.0 CE A:MSE238 2.8 70.8 1.0 ZN A:ZN507 3.0 59.1 1.0 CE1 A:HIS466 3.0 28.6 1.0 OE2 A:GLU236 3.2 45.3 1.0 CD2 A:HIS466 3.3 27.6 1.0 O A:HOH2131 3.9 11.6 1.0 SE A:MSE238 4.0 77.8 0.5 CD A:GLU236 4.1 44.4 1.0 ND1 A:HIS466 4.2 28.2 1.0 CG A:GLU236 4.2 38.9 1.0 CG A:HIS466 4.3 26.2 1.0 NE1 A:TRP474 4.5 36.7 1.0 CG A:MSE238 4.7 56.7 1.0 CD1 A:TRP474 4.7 33.3 1.0 CB A:GLU236 4.8 32.7 1.0 O A:PHE473 4.9 25.2 1.0

Zinc binding site 8 out of 12 in the Crystal Structure of Ylib Protein From Escherichia Coi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of Ylib Protein From Escherichia Coi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn507 b:59.1 occ:1.00 OE2 A:GLU236 2.5 45.3 1.0 CE1 A:HIS466 2.6 28.6 1.0 ZN A:ZN506 3.0 67.7 1.0 NE2 A:HIS466 3.2 28.6 1.0 CD A:GLU236 3.4 44.4 1.0 ND1 A:HIS466 3.7 28.2 1.0 O A:HOH2131 3.9 11.6 1.0 O A:LEU470 4.0 18.2 1.0 OE1 A:GLU236 4.0 44.3 1.0 CG A:GLU236 4.3 38.9 1.0 CD2 A:HIS466 4.4 27.6 1.0 CB A:GLU236 4.5 32.7 1.0 CG2 A:THR471 4.6 15.3 1.0 O A:HOH2132 4.7 23.5 1.0 CG A:HIS466 4.7 26.2 1.0 O A:LYS468 4.9 22.6 1.0

Zinc binding site 9 out of 12 in the Crystal Structure of Ylib Protein From Escherichia Coi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Crystal Structure of Ylib Protein From Escherichia Coi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn508 b:39.6 occ:1.00 OD1 A:ASP307 2.2 31.2 1.0 CG A:ASP307 3.1 31.4 1.0 OD2 A:ASP307 3.3 33.6 1.0 CB A:LYS310 4.0 40.3 1.0 N A:LYS310 4.2 37.2 1.0 CA A:LYS310 4.4 39.8 1.0 CB A:ASP307 4.5 28.7 1.0 CB A:VAL309 4.6 32.9 1.0 CG1 A:VAL309 4.7 31.2 1.0

Zinc binding site 10 out of 12 in the Crystal Structure of Ylib Protein From Escherichia Coi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Crystal Structure of Ylib Protein From Escherichia Coi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn509 b:44.0 occ:1.00 NE2 A:HIS334 2.2 50.7 1.0 NE2 A:HIS332 2.3 57.3 1.0 O A:HOH2151 2.4 29.6 1.0 CE1 A:HIS334 2.9 50.3 1.0 CE1 A:HIS332 3.0 57.2 1.0 CD2 A:HIS334 3.3 50.8 1.0 CD2 A:HIS332 3.4 56.5 1.0 ND1 A:HIS334 4.0 50.6 1.0 ND1 A:HIS332 4.2 58.2 1.0 CG A:HIS334 4.2 51.0 1.0 CG A:HIS332 4.4 56.5 1.0

S.Jeudy, C.Abergel, J.M.Claverie. Crystal Structure of Ylib Protein From E.Coli To Be Published.