Zinc in PDB 2i0o: Crystal Structure of Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+

The structure of Crystal Structure of Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+, PDB code: 2i0o was solved by X.Jin, J.M.Sauder, S.K.Burley, L.Shapiro, New York Sgx Research Centerfor Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	64.109, 84.572, 108.279, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 23.5

The binding sites of Zinc atom in the Crystal Structure of Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+ (pdb code 2i0o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Crystal Structure of Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+, PDB code: 2i0o:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the Crystal Structure of Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+


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 Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn579 b:22.7 occ:1.00 OD2 A:ASP425 2.0 28.2 1.0 OD2 A:ASP518 2.0 30.0 1.0 NE2 A:HIS59 2.0 22.3 1.0 O A:HOH932 2.2 26.3 1.0 CG A:ASP425 2.8 24.5 1.0 OD1 A:ASP425 2.9 20.4 1.0 CD2 A:HIS59 3.0 24.1 1.0 CE1 A:HIS59 3.0 21.8 1.0 CG A:ASP518 3.1 24.1 1.0 O A:HOH968 3.7 52.3 1.0 CB A:ASP518 3.8 21.6 1.0 O A:HOH796 3.8 45.9 1.0 O A:HOH779 3.9 35.2 1.0 ND1 A:HIS59 4.1 21.6 1.0 CG A:HIS59 4.1 21.6 1.0 OD1 A:ASP518 4.2 29.8 1.0 CB A:ASP425 4.2 21.0 1.0 CD2 A:LEU473 4.3 23.1 0.5 O A:HOH602 4.5 19.2 1.0 O A:HOH950 4.5 19.9 1.0 ZN A:ZN580 4.5 30.9 1.0 OD2 A:ASP57 4.7 21.8 1.0 OD1 A:ASN472 5.0 34.0 1.0

Zinc binding site 2 out of 6 in the Crystal Structure of Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+


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 Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn580 b:30.9 occ:1.00 OE2 A:GLU37 1.9 18.0 1.0 OD2 A:ASP57 2.0 21.8 1.0 O A:HOH950 2.1 19.9 1.0 OD1 A:ASP518 2.2 29.8 1.0 O A:HOH919 2.5 18.2 1.0 CG A:ASP57 2.8 24.9 1.0 OD1 A:ASP57 2.8 20.9 1.0 CG A:ASP518 2.9 24.1 1.0 OD2 A:ASP518 3.0 30.0 1.0 O A:HOH961 3.1 38.4 1.0 CD A:GLU37 3.3 32.1 1.0 ZN A:ZN581 3.6 23.7 1.0 O A:HOH594 3.7 12.4 1.0 O A:HOH847 4.1 44.8 1.0 OE1 A:GLU37 4.1 31.8 1.0 O A:HOH602 4.1 19.2 1.0 CE1 A:HIS59 4.2 21.8 1.0 CB A:ASP57 4.2 21.1 1.0 NE2 A:HIS59 4.3 22.3 1.0 OD1 A:ASP38 4.3 27.5 1.0 CG A:GLU37 4.4 33.1 1.0 CB A:ASP518 4.4 21.6 1.0 ND1 A:HIS59 4.5 21.6 1.0 ZN A:ZN579 4.5 22.7 1.0 N A:ASP518 4.6 18.6 1.0 CB A:CYS517 4.6 18.0 1.0 SG A:CYS517 4.6 21.4 1.0 N A:GLY519 4.6 22.2 1.0 CD2 A:HIS59 4.7 24.1 1.0 O A:ASN569 4.8 32.5 1.0 O A:HOH968 4.9 52.3 1.0 O A:HOH636 4.9 22.9 1.0 CG A:HIS59 4.9 21.6 1.0 CA A:ASP518 4.9 20.7 1.0

Zinc binding site 3 out of 6 in the Crystal Structure of Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+


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 Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn581 b:23.7 occ:1.00 OD2 A:ASP38 2.0 31.7 1.0 O A:ASN569 2.0 32.5 1.0 O A:HOH919 2.2 18.2 1.0 SG A:CYS517 2.4 21.4 1.0 CG A:ASP38 2.7 26.6 1.0 OD1 A:ASP38 2.8 27.5 1.0 C A:ASN569 3.1 32.9 1.0 CB A:CYS517 3.2 18.0 1.0 O A:HOH961 3.4 38.4 1.0 ZN A:ZN580 3.6 30.9 1.0 OE2 A:GLU37 3.9 18.0 1.0 OD2 A:ASP57 3.9 21.8 1.0 N A:MET570 3.9 31.6 1.0 CA A:MET570 3.9 32.8 1.0 CB A:ASN569 4.1 34.6 1.0 N A:THR571 4.2 26.1 1.0 CA A:ASN569 4.2 33.5 1.0 CB A:ASP38 4.2 24.1 1.0 CG A:ASP57 4.3 24.9 1.0 OD1 A:ASP518 4.3 29.8 1.0 C A:MET570 4.4 28.6 1.0 CG A:GLU37 4.5 33.1 1.0 OG1 A:THR571 4.6 25.5 1.0 CD A:GLU37 4.6 32.1 1.0 OD1 A:ASP57 4.6 20.9 1.0 CA A:CYS517 4.6 18.1 1.0 N A:GLY519 4.8 22.2 1.0 N A:ASN569 4.8 33.4 1.0 CB A:THR571 4.8 24.1 1.0

Zinc binding site 4 out of 6 in the Crystal Structure of Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+


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 Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn582 b:34.4 occ:1.00 OE1 A:GLN452 2.0 26.1 1.0 OE1 A:GLU455 2.0 32.9 1.0 O A:HOH767 2.4 36.1 1.0 CD A:GLN452 3.0 30.9 1.0 CD A:GLU455 3.0 32.8 1.0 NE2 A:GLN452 3.5 32.7 1.0 OE2 A:GLU455 3.5 32.5 1.0 CG A:GLN452 4.3 24.6 1.0 CG A:GLU455 4.3 29.2 1.0 CA A:GLN452 4.6 20.9 1.0 CD2 A:TYR451 4.7 21.5 1.0 CB A:GLU455 4.7 24.0 1.0 CB A:GLN452 4.8 22.7 1.0 CE2 A:TYR451 4.8 24.7 1.0

Zinc binding site 5 out of 6 in the Crystal Structure of Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+


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 Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn583 b:19.3 occ:0.50 NE2 A:HIS71 2.0 20.8 1.0 OE2 A:GLU110 2.0 18.5 1.0 CD A:GLU110 2.8 20.0 1.0 OE1 A:GLU110 2.9 19.8 1.0 CD2 A:HIS71 2.9 25.4 1.0 CE1 A:HIS71 2.9 28.1 1.0 ND1 A:HIS71 4.0 28.4 1.0 CG A:HIS71 4.1 22.1 1.0 CG A:GLU110 4.3 17.6 1.0 CB A:LEU70 4.6 20.8 1.0 O A:HOH607 4.7 30.4 1.0 CE1 A:TYR67 4.8 22.1 1.0 O A:HOH771 4.9 25.3 1.0 CD1 A:LEU70 5.0 21.4 1.0

Zinc binding site 6 out of 6 in the Crystal Structure of Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+


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 Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn584 b:40.4 occ:1.00 O A:HOH928 2.1 33.7 1.0 NE2 A:HIS40 2.2 27.8 1.0 O A:HOH911 2.2 41.8 1.0 O A:HOH593 2.3 24.0 1.0 O A:HOH940 2.5 44.0 1.0 CE1 A:HIS40 2.9 28.6 1.0 CD2 A:HIS40 3.2 27.5 1.0 OG A:SER26 3.9 25.9 1.0 O A:HOH637 4.0 27.6 1.0 O A:HOH738 4.0 33.0 1.0 ND1 A:HIS40 4.1 25.0 1.0 CG A:HIS40 4.2 24.3 1.0 O A:HOH775 4.4 38.2 1.0 O A:HOH718 4.5 36.0 1.0 SG A:CYS42 4.7 29.3 0.5 CB A:CYS42 4.9 25.9 0.5 CB A:SER15 4.9 28.0 1.0 CB A:CYS42 4.9 26.4 0.5

S.C.Almo, J.B.Bonanno, J.M.Sauder, S.Emtage, T.P.Dilorenzo, V.Malashkevich, S.R.Wasserman, S.Swaminathan, S.Eswaramoorthy, R.Agarwal, D.Kumaran, M.Madegowda, S.Ragumani, Y.Patskovsky, J.Alvarado, U.A.Ramagopal, J.Faber-Barata, M.R.Chance, A.Sali, A.Fiser, Z.Y.Zhang, D.S.Lawrence, S.K.Burley. Structural Genomics of Protein Phosphatases. J.Struct.Funct.Genom. V. 8 121 2007.
ISSN: ISSN 1345-711X
PubMed: 18058037
DOI: 10.1007/S10969-007-9036-1