Zinc in PDB 2i0o: Crystal Structure of Anopheles Gambiae Ser/Thr Phosphatase Complexed with ZN2+
Protein crystallography data
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
|
Zinc Binding Sites:
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 2i0o
Go back to
Zinc Binding Sites List in 2i0o
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 2i0o
Go back to
Zinc Binding Sites List in 2i0o
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 2i0o
Go back to
Zinc Binding Sites List in 2i0o
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 2i0o
Go back to
Zinc Binding Sites List in 2i0o
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 2i0o
Go back to
Zinc Binding Sites List in 2i0o
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 2i0o
Go back to
Zinc Binding Sites List in 2i0o
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
|
|
Reference:
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
Page generated: Thu Oct 17 00:45:32 2024
|