Zinc in PDB 1j2t: Creatininase Mn
Enzymatic activity of Creatininase Mn
All present enzymatic activity of Creatininase Mn:
3.5.2.10;
Protein crystallography data
The structure of Creatininase Mn, PDB code: 1j2t
was solved by
T.Yoshimoto,
N.Tanaka,
N.Kanada,
T.Inoue,
Y.Nakajima,
M.Haratake,
K.T.Nakamura,
Y.Xu,
K.Ito,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.00 /
1.80
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
101.989,
150.742,
167.066,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.5 /
19.3
|
Other elements in 1j2t:
The structure of Creatininase Mn also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Creatininase Mn
(pdb code 1j2t). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
Creatininase Mn, PDB code: 1j2t:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 1j2t
Go back to
Zinc Binding Sites List in 1j2t
Zinc binding site 1 out
of 6 in the Creatininase Mn
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Creatininase Mn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn302
b:16.9
occ:1.00
|
O
|
A:HOH7008
|
1.9
|
14.4
|
1.0
|
OE1
|
A:GLU183
|
2.0
|
16.7
|
1.0
|
OD1
|
A:ASP45
|
2.0
|
14.6
|
1.0
|
NE2
|
A:HIS36
|
2.1
|
15.3
|
1.0
|
CD
|
A:GLU183
|
2.7
|
14.9
|
1.0
|
OE2
|
A:GLU183
|
2.8
|
15.4
|
1.0
|
CG
|
A:ASP45
|
3.0
|
14.5
|
1.0
|
CE1
|
A:HIS36
|
3.0
|
14.0
|
1.0
|
CD2
|
A:HIS36
|
3.1
|
15.9
|
1.0
|
OD2
|
A:ASP45
|
3.2
|
14.6
|
1.0
|
MN
|
A:MN301
|
3.5
|
15.0
|
1.0
|
O
|
A:HOH7010
|
3.8
|
20.9
|
1.0
|
ND1
|
A:HIS178
|
3.9
|
17.7
|
1.0
|
O
|
A:HOH7011
|
3.9
|
17.9
|
1.0
|
OE2
|
A:GLU34
|
4.0
|
15.3
|
1.0
|
CG1
|
A:VAL44
|
4.1
|
15.6
|
1.0
|
CE1
|
A:HIS178
|
4.1
|
15.3
|
1.0
|
ND1
|
A:HIS36
|
4.1
|
14.7
|
1.0
|
CG
|
A:GLU183
|
4.2
|
15.8
|
1.0
|
CG
|
A:HIS36
|
4.2
|
15.6
|
1.0
|
CB
|
A:ASP45
|
4.4
|
13.9
|
1.0
|
O
|
A:GLY119
|
4.5
|
14.5
|
1.0
|
N
|
A:ASP45
|
4.6
|
13.8
|
1.0
|
CB
|
A:VAL44
|
4.6
|
14.9
|
1.0
|
CA
|
A:ASP45
|
4.7
|
14.1
|
1.0
|
O
|
A:HOH7009
|
4.8
|
17.3
|
1.0
|
O
|
A:HOH7025
|
4.9
|
13.3
|
1.0
|
|
Zinc binding site 2 out
of 6 in 1j2t
Go back to
Zinc Binding Sites List in 1j2t
Zinc binding site 2 out
of 6 in the Creatininase Mn
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Creatininase Mn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn302
b:20.6
occ:1.00
|
O
|
B:HOH7009
|
1.9
|
17.6
|
1.0
|
OE1
|
B:GLU183
|
1.9
|
20.6
|
1.0
|
NE2
|
B:HIS36
|
2.0
|
19.3
|
1.0
|
OD1
|
B:ASP45
|
2.1
|
17.5
|
1.0
|
CD
|
B:GLU183
|
2.7
|
21.1
|
1.0
|
OE2
|
B:GLU183
|
2.8
|
19.9
|
1.0
|
CE1
|
B:HIS36
|
2.9
|
16.6
|
1.0
|
CG
|
B:ASP45
|
3.0
|
17.3
|
1.0
|
CD2
|
B:HIS36
|
3.1
|
18.1
|
1.0
|
OD2
|
B:ASP45
|
3.1
|
18.1
|
1.0
|
MN
|
B:MN301
|
3.5
|
17.9
|
1.0
|
ND1
|
B:HIS178
|
3.7
|
22.0
|
1.0
|
CE1
|
B:HIS178
|
4.0
|
20.4
|
1.0
|
O
|
B:HOH7012
|
4.0
|
18.3
|
1.0
|
O
|
B:HOH7011
|
4.0
|
26.2
|
1.0
|
OE2
|
B:GLU34
|
4.0
|
17.6
|
1.0
|
ND1
|
B:HIS36
|
4.1
|
17.3
|
1.0
|
CG1
|
B:VAL44
|
4.1
|
18.2
|
1.0
|
CG
|
B:GLU183
|
4.2
|
21.5
|
1.0
|
CG
|
B:HIS36
|
4.2
|
18.8
|
1.0
|
CB
|
B:ASP45
|
4.4
|
17.3
|
1.0
|
O
|
B:GLY119
|
4.5
|
17.3
|
1.0
|
CB
|
B:VAL44
|
4.6
|
17.4
|
1.0
|
N
|
B:ASP45
|
4.6
|
17.4
|
1.0
|
CA
|
B:ASP45
|
4.7
|
17.2
|
1.0
|
O
|
B:HOH7010
|
4.9
|
19.2
|
1.0
|
O
|
B:HOH7047
|
4.9
|
18.1
|
1.0
|
|
Zinc binding site 3 out
of 6 in 1j2t
Go back to
Zinc Binding Sites List in 1j2t
Zinc binding site 3 out
of 6 in the Creatininase Mn
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Creatininase Mn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn302
b:20.1
occ:1.00
|
OE1
|
C:GLU183
|
1.9
|
19.9
|
1.0
|
O
|
C:HOH7010
|
2.0
|
16.1
|
1.0
|
NE2
|
C:HIS36
|
2.0
|
17.0
|
1.0
|
OD1
|
C:ASP45
|
2.0
|
19.8
|
1.0
|
CD
|
C:GLU183
|
2.7
|
18.0
|
1.0
|
OE2
|
C:GLU183
|
2.9
|
18.7
|
1.0
|
CE1
|
C:HIS36
|
2.9
|
17.4
|
1.0
|
CG
|
C:ASP45
|
3.0
|
18.7
|
1.0
|
CD2
|
C:HIS36
|
3.1
|
18.2
|
1.0
|
OD2
|
C:ASP45
|
3.2
|
16.0
|
1.0
|
MN
|
C:MN301
|
3.5
|
17.6
|
1.0
|
ND1
|
C:HIS178
|
3.7
|
19.2
|
1.0
|
CE1
|
C:HIS178
|
4.0
|
18.0
|
1.0
|
O
|
C:HOH7013
|
4.0
|
20.6
|
1.0
|
ND1
|
C:HIS36
|
4.1
|
16.6
|
1.0
|
O
|
C:HOH7012
|
4.1
|
29.7
|
1.0
|
OE2
|
C:GLU34
|
4.1
|
15.6
|
1.0
|
CG
|
C:GLU183
|
4.2
|
19.2
|
1.0
|
CG
|
C:HIS36
|
4.2
|
17.6
|
1.0
|
CG1
|
C:VAL44
|
4.2
|
17.5
|
1.0
|
CB
|
C:ASP45
|
4.4
|
17.4
|
1.0
|
O
|
C:GLY119
|
4.6
|
16.9
|
1.0
|
CB
|
C:VAL44
|
4.6
|
16.9
|
1.0
|
O
|
C:HOH7170
|
4.6
|
49.9
|
1.0
|
N
|
C:ASP45
|
4.7
|
17.1
|
1.0
|
CA
|
C:ASP45
|
4.7
|
17.1
|
1.0
|
O
|
C:HOH7011
|
4.8
|
16.8
|
1.0
|
O
|
C:HOH7017
|
5.0
|
15.6
|
1.0
|
|
Zinc binding site 4 out
of 6 in 1j2t
Go back to
Zinc Binding Sites List in 1j2t
Zinc binding site 4 out
of 6 in the Creatininase Mn
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Creatininase Mn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn302
b:21.1
occ:1.00
|
OE1
|
D:GLU183
|
1.9
|
20.4
|
1.0
|
NE2
|
D:HIS36
|
2.0
|
20.1
|
1.0
|
OD1
|
D:ASP45
|
2.0
|
19.4
|
1.0
|
O
|
D:HOH7002
|
2.0
|
19.7
|
1.0
|
CD
|
D:GLU183
|
2.7
|
21.1
|
1.0
|
OE2
|
D:GLU183
|
2.8
|
20.2
|
1.0
|
CE1
|
D:HIS36
|
2.9
|
20.0
|
1.0
|
CG
|
D:ASP45
|
3.0
|
19.8
|
1.0
|
CD2
|
D:HIS36
|
3.1
|
20.6
|
1.0
|
OD2
|
D:ASP45
|
3.2
|
19.5
|
1.0
|
MN
|
D:MN301
|
3.5
|
18.8
|
1.0
|
O
|
D:HOH7004
|
3.7
|
24.8
|
1.0
|
ND1
|
D:HIS178
|
3.8
|
17.5
|
1.0
|
O
|
D:HOH7005
|
3.9
|
23.1
|
1.0
|
ND1
|
D:HIS36
|
4.1
|
19.9
|
1.0
|
CE1
|
D:HIS178
|
4.1
|
16.1
|
1.0
|
OE2
|
D:GLU34
|
4.1
|
18.2
|
1.0
|
CG
|
D:GLU183
|
4.1
|
22.3
|
1.0
|
CG
|
D:HIS36
|
4.2
|
20.0
|
1.0
|
CG1
|
D:VAL44
|
4.2
|
18.6
|
1.0
|
CB
|
D:ASP45
|
4.3
|
18.3
|
1.0
|
O
|
D:GLY119
|
4.5
|
17.2
|
1.0
|
CB
|
D:VAL44
|
4.6
|
17.9
|
1.0
|
N
|
D:ASP45
|
4.6
|
18.6
|
1.0
|
CA
|
D:ASP45
|
4.7
|
18.6
|
1.0
|
O
|
D:HOH7003
|
4.9
|
18.1
|
1.0
|
O
|
D:HOH7014
|
5.0
|
19.9
|
1.0
|
|
Zinc binding site 5 out
of 6 in 1j2t
Go back to
Zinc Binding Sites List in 1j2t
Zinc binding site 5 out
of 6 in the Creatininase Mn
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Creatininase Mn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn302
b:20.8
occ:1.00
|
OE1
|
E:GLU183
|
1.9
|
22.6
|
1.0
|
NE2
|
E:HIS36
|
2.0
|
19.5
|
1.0
|
OD1
|
E:ASP45
|
2.0
|
18.4
|
1.0
|
O
|
E:HOH7004
|
2.1
|
18.8
|
1.0
|
CD
|
E:GLU183
|
2.6
|
21.1
|
1.0
|
OE2
|
E:GLU183
|
2.7
|
19.1
|
1.0
|
CE1
|
E:HIS36
|
2.9
|
19.1
|
1.0
|
CG
|
E:ASP45
|
3.0
|
18.1
|
1.0
|
CD2
|
E:HIS36
|
3.0
|
18.9
|
1.0
|
OD2
|
E:ASP45
|
3.1
|
17.4
|
1.0
|
MN
|
E:MN301
|
3.5
|
18.2
|
1.0
|
O
|
E:HOH7006
|
3.7
|
25.5
|
1.0
|
ND1
|
E:HIS178
|
3.8
|
19.4
|
1.0
|
O
|
E:HOH7007
|
4.0
|
19.4
|
1.0
|
ND1
|
E:HIS36
|
4.0
|
18.8
|
1.0
|
CE1
|
E:HIS178
|
4.1
|
17.1
|
1.0
|
CG
|
E:GLU183
|
4.1
|
22.6
|
1.0
|
CG
|
E:HIS36
|
4.1
|
18.8
|
1.0
|
CG1
|
E:VAL44
|
4.2
|
19.2
|
1.0
|
OE2
|
E:GLU34
|
4.2
|
15.8
|
1.0
|
CB
|
E:ASP45
|
4.4
|
18.2
|
1.0
|
O
|
E:GLY119
|
4.5
|
17.3
|
1.0
|
N
|
E:ASP45
|
4.6
|
18.4
|
1.0
|
CB
|
E:VAL44
|
4.6
|
18.4
|
1.0
|
CA
|
E:ASP45
|
4.7
|
18.3
|
1.0
|
O
|
E:HOH7005
|
4.8
|
17.2
|
1.0
|
CB
|
E:GLU183
|
4.9
|
21.9
|
1.0
|
O
|
E:HOH7018
|
4.9
|
18.5
|
1.0
|
|
Zinc binding site 6 out
of 6 in 1j2t
Go back to
Zinc Binding Sites List in 1j2t
Zinc binding site 6 out
of 6 in the Creatininase Mn
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Creatininase Mn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Zn302
b:19.2
occ:1.00
|
O
|
F:HOH7011
|
1.9
|
15.7
|
1.0
|
OE1
|
F:GLU183
|
2.0
|
17.4
|
1.0
|
OD1
|
F:ASP45
|
2.0
|
14.9
|
1.0
|
NE2
|
F:HIS36
|
2.0
|
18.9
|
1.0
|
CD
|
F:GLU183
|
2.7
|
18.0
|
1.0
|
OE2
|
F:GLU183
|
2.8
|
17.7
|
1.0
|
CG
|
F:ASP45
|
3.0
|
15.2
|
1.0
|
CE1
|
F:HIS36
|
3.0
|
17.8
|
1.0
|
CD2
|
F:HIS36
|
3.0
|
18.2
|
1.0
|
OD2
|
F:ASP45
|
3.2
|
14.9
|
1.0
|
MN
|
F:MN301
|
3.5
|
16.8
|
1.0
|
ND1
|
F:HIS178
|
3.8
|
17.6
|
1.0
|
O
|
F:HOH7014
|
3.9
|
19.3
|
1.0
|
CE1
|
F:HIS178
|
4.0
|
17.8
|
1.0
|
O
|
F:HOH7013
|
4.1
|
28.6
|
1.0
|
ND1
|
F:HIS36
|
4.1
|
17.4
|
1.0
|
CG1
|
F:VAL44
|
4.1
|
18.1
|
1.0
|
OE2
|
F:GLU34
|
4.1
|
16.8
|
1.0
|
CG
|
F:HIS36
|
4.2
|
18.6
|
1.0
|
CG
|
F:GLU183
|
4.2
|
17.2
|
1.0
|
CB
|
F:ASP45
|
4.4
|
14.9
|
1.0
|
O
|
F:HOH7189
|
4.4
|
45.3
|
1.0
|
O
|
F:GLY119
|
4.5
|
15.7
|
1.0
|
CB
|
F:VAL44
|
4.6
|
16.6
|
1.0
|
N
|
F:ASP45
|
4.6
|
15.4
|
1.0
|
CA
|
F:ASP45
|
4.7
|
15.0
|
1.0
|
O
|
F:HOH7012
|
4.9
|
17.7
|
1.0
|
O
|
F:HOH7026
|
5.0
|
15.6
|
1.0
|
|
Reference:
T.Yoshimoto,
N.Tanaka,
N.Kanada,
T.Inoue,
Y.Nakajima,
M.Haratake,
K.T.Nakamura,
Y.Xu,
K.Ito.
Crystal Structures of Creatininase Reveal the Substrate Binding Site and Provide An Insight Into the Catalytic Mechanism J.Mol.Biol. V. 337 399 2004.
ISSN: ISSN 0022-2836
PubMed: 15003455
DOI: 10.1016/J.JMB.2004.01.022
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