Zinc in PDB 1l7o: Crystal Structure of Phosphoserine Phosphatase in Apo Form

All present enzymatic activity of Crystal Structure of Phosphoserine Phosphatase in Apo Form:
3.1.3.3;

The structure of Crystal Structure of Phosphoserine Phosphatase in Apo Form, PDB code: 1l7o was solved by W.Wang, H.S.Cho, R.Kim, J.Jancarik, H.Yokota, H.H.Nguyen, I.V.Grigoriev, D.E.Wemmer, S.H.Kim, Berkeley Structural Genomics Center (Bsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.888, 117.889, 117.361, 90.00, 90.00, 90.00
R / Rfree (%)	22.4 / 25.4

The binding sites of Zinc atom in the Crystal Structure of Phosphoserine Phosphatase in Apo Form (pdb code 1l7o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of Phosphoserine Phosphatase in Apo Form, PDB code: 1l7o:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of Phosphoserine Phosphatase in Apo Form


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 Phosphoserine Phosphatase in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:44.6 occ:1.00 OE1 A:GLU79 2.2 45.0 1.0 OE2 A:GLU79 2.5 42.0 1.0 CD A:GLU79 2.7 40.9 1.0 O A:ACY312 2.9 43.0 1.0 C A:ACY312 3.4 42.0 1.0 CH3 A:ACY312 3.5 43.8 1.0 CG A:GLU79 4.2 36.6 1.0 OXT A:ACY312 4.3 46.5 1.0 NH2 A:ARG204 4.3 44.1 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of Phosphoserine Phosphatase in Apo Form


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 Phosphoserine Phosphatase in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:27.9 occ:1.00 OE2 B:GLU699 2.1 26.0 1.0 OE2 A:GLU199 2.2 28.5 1.0 SG B:CYS697 2.3 28.1 1.0 SG A:CYS197 2.4 24.7 1.0 CD A:GLU199 3.0 28.6 1.0 CD B:GLU699 3.1 26.7 1.0 CG A:GLU199 3.2 28.2 1.0 CG B:GLU699 3.3 24.2 1.0 CB B:CYS697 3.4 24.7 1.0 CB A:CYS197 3.4 22.8 1.0 CD A:LYS191 4.1 34.0 1.0 CD B:LYS691 4.1 28.3 1.0 OE1 A:GLU199 4.2 32.0 1.0 OE1 B:GLU699 4.2 28.6 1.0 CE B:LYS691 4.3 31.8 1.0 NZ A:LYS191 4.4 34.5 1.0 CE A:LYS191 4.5 33.2 1.0 NZ B:LYS691 4.6 33.4 1.0 O B:CYS697 4.6 23.0 1.0 CG B:LYS691 4.7 30.6 1.0 O A:CYS197 4.7 24.5 1.0 CA B:CYS697 4.7 25.5 1.0 CA A:CYS197 4.7 23.1 1.0 C B:CYS697 4.7 24.3 1.0 C A:CYS197 4.7 23.9 1.0 CG A:LYS191 4.7 33.2 1.0 CB A:GLU199 4.7 25.9 1.0 O B:HOH2008 4.7 21.5 1.0 CB B:GLU699 4.8 25.6 1.0 CB A:LYS191 4.9 33.1 1.0 O A:HOH2013 5.0 27.5 1.0 CB B:LYS691 5.0 30.4 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of Phosphoserine Phosphatase in Apo Form


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 Phosphoserine Phosphatase in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn303 b:37.8 occ:1.00 OE2 B:GLU579 2.2 27.2 1.0 O B:ACY311 2.4 29.1 1.0 OE1 B:GLU579 2.6 27.5 1.0 CD B:GLU579 2.7 27.1 1.0 C B:ACY311 3.3 25.0 1.0 NH2 B:ARG704 3.9 33.9 1.0 OXT B:ACY311 4.0 29.5 1.0 CH3 B:ACY311 4.2 30.4 1.0 CG B:GLU579 4.2 26.0 1.0 CZ B:ARG704 5.0 33.1 1.0

W.Wang, H.S.Cho, R.Kim, J.Jancarik, H.Yokota, H.H.Nguyen, I.V.Grigoriev, D.E.Wemmer, S.H.Kim. Structural Characterization of the Reaction Pathway in Phosphoserine Phosphatase: Crystallographic "Snapshots" of Intermediate States. J.Mol.Biol. V. 319 421 2002.
ISSN: ISSN 0022-2836
PubMed: 12051918
DOI: 10.1016/S0022-2836(02)00324-8