Zinc in PDB 9dr5: Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form)
Enzymatic activity of Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form)
All present enzymatic activity of Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form):
1.13.11.1;
Protein crystallography data
The structure of Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form), PDB code: 9dr5
was solved by
Seattle Structural Genomics Center For Infectious Disease,
Seattlestructural Genomics Center For Infectious Disease (Ssgcid),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
51.99 /
1.71
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
84.97,
86.27,
110.161,
106.04,
96.74,
113.15
|
R / Rfree (%)
|
15.1 /
18.3
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form)
(pdb code 9dr5). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the
Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form), PDB code: 9dr5:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Zinc binding site 1 out
of 8 in 9dr5
Go back to
Zinc Binding Sites List in 9dr5
Zinc binding site 1 out
of 8 in the Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 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 Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn401
b:27.1
occ:0.66
|
OXT
|
A:ACT406
|
1.9
|
24.5
|
0.7
|
OH
|
A:TYR164
|
1.9
|
19.5
|
1.0
|
NE2
|
A:HIS224
|
2.2
|
22.4
|
1.0
|
NE2
|
A:HIS226
|
2.2
|
21.4
|
1.0
|
OH
|
A:TYR200
|
2.4
|
19.5
|
0.3
|
C
|
A:ACT406
|
2.6
|
23.8
|
0.7
|
O
|
A:ACT406
|
2.9
|
23.7
|
0.7
|
CZ
|
A:TYR164
|
2.9
|
21.9
|
1.0
|
CD2
|
A:HIS226
|
2.9
|
21.9
|
1.0
|
CE1
|
A:HIS224
|
3.0
|
24.4
|
1.0
|
CD2
|
A:HIS224
|
3.3
|
27.8
|
1.0
|
CE1
|
A:HIS226
|
3.3
|
19.6
|
1.0
|
CE1
|
A:TYR164
|
3.6
|
20.3
|
1.0
|
CZ
|
A:TYR200
|
3.6
|
18.6
|
0.3
|
NH1
|
A:ARG221
|
3.6
|
29.6
|
1.0
|
CE2
|
A:TYR164
|
3.8
|
17.9
|
1.0
|
CE2
|
A:TYR200
|
4.0
|
21.8
|
0.3
|
O
|
A:HOH518
|
4.0
|
18.1
|
1.0
|
CH3
|
A:ACT406
|
4.0
|
22.2
|
0.7
|
CG
|
A:HIS226
|
4.2
|
17.0
|
1.0
|
ND1
|
A:HIS224
|
4.2
|
24.0
|
1.0
|
ND1
|
A:HIS226
|
4.3
|
19.9
|
1.0
|
CG
|
A:HIS224
|
4.3
|
20.1
|
1.0
|
O
|
A:HOH565
|
4.5
|
19.7
|
1.0
|
CZ
|
A:ARG221
|
4.7
|
33.2
|
1.0
|
CE1
|
A:TYR200
|
4.8
|
19.6
|
0.3
|
CD1
|
A:TYR164
|
4.9
|
22.7
|
1.0
|
CD
|
A:ARG221
|
5.0
|
22.5
|
1.0
|
|
Zinc binding site 2 out
of 8 in 9dr5
Go back to
Zinc Binding Sites List in 9dr5
Zinc binding site 2 out
of 8 in the Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 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 Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn401
b:23.3
occ:0.52
|
OH
|
B:TYR164
|
1.8
|
18.9
|
1.0
|
OXT
|
B:ACT404
|
2.0
|
24.7
|
0.5
|
NE2
|
B:HIS226
|
2.2
|
22.7
|
1.0
|
NE2
|
B:HIS224
|
2.3
|
20.2
|
1.0
|
OH
|
B:TYR200
|
2.5
|
18.6
|
0.5
|
C
|
B:ACT404
|
2.6
|
21.8
|
0.5
|
O
|
B:ACT404
|
2.7
|
17.8
|
0.5
|
CZ
|
B:TYR164
|
2.9
|
18.8
|
1.0
|
CD2
|
B:HIS226
|
2.9
|
21.6
|
1.0
|
CE1
|
B:HIS224
|
3.1
|
22.3
|
1.0
|
CE1
|
B:HIS226
|
3.3
|
25.0
|
1.0
|
CD2
|
B:HIS224
|
3.3
|
25.8
|
1.0
|
CE1
|
B:TYR164
|
3.7
|
20.7
|
1.0
|
CZ
|
B:TYR200
|
3.7
|
20.9
|
0.5
|
CE2
|
B:TYR164
|
3.7
|
17.0
|
1.0
|
NH1
|
B:ARG221
|
3.7
|
29.0
|
1.0
|
O
|
B:HOH538
|
4.0
|
16.8
|
1.0
|
CH3
|
B:ACT404
|
4.0
|
22.1
|
0.5
|
CE2
|
B:TYR200
|
4.2
|
20.6
|
0.5
|
CG
|
B:HIS226
|
4.2
|
17.9
|
1.0
|
ND1
|
B:HIS224
|
4.2
|
21.9
|
1.0
|
ND1
|
B:HIS226
|
4.3
|
20.4
|
1.0
|
CG
|
B:HIS224
|
4.4
|
20.0
|
1.0
|
O
|
B:HOH627
|
4.5
|
17.1
|
1.0
|
CZ
|
B:ARG221
|
4.8
|
27.2
|
1.0
|
CE1
|
B:TYR200
|
4.8
|
21.0
|
0.5
|
CD1
|
B:TYR164
|
4.9
|
20.5
|
1.0
|
CD2
|
B:TYR164
|
5.0
|
17.6
|
1.0
|
|
Zinc binding site 3 out
of 8 in 9dr5
Go back to
Zinc Binding Sites List in 9dr5
Zinc binding site 3 out
of 8 in the Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 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 Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn401
b:29.7
occ:0.69
|
OH
|
C:TYR164
|
1.9
|
22.4
|
1.0
|
OXT
|
C:ACT406
|
2.0
|
22.9
|
0.7
|
NE2
|
C:HIS226
|
2.2
|
22.1
|
1.0
|
NE2
|
C:HIS224
|
2.3
|
23.9
|
1.0
|
OH
|
C:TYR200
|
2.3
|
21.6
|
0.3
|
C
|
C:ACT406
|
2.7
|
22.8
|
0.7
|
O
|
C:ACT406
|
2.9
|
22.1
|
0.7
|
CZ
|
C:TYR164
|
2.9
|
21.6
|
1.0
|
CD2
|
C:HIS226
|
3.0
|
21.7
|
1.0
|
CE1
|
C:HIS224
|
3.0
|
28.5
|
1.0
|
CE1
|
C:HIS226
|
3.3
|
21.0
|
1.0
|
CD2
|
C:HIS224
|
3.4
|
28.5
|
1.0
|
CZ
|
C:TYR200
|
3.6
|
22.5
|
0.3
|
CE1
|
C:TYR164
|
3.6
|
22.4
|
1.0
|
NH1
|
C:ARG221
|
3.7
|
29.2
|
1.0
|
CE2
|
C:TYR164
|
3.8
|
19.9
|
1.0
|
O
|
C:HOH519
|
4.0
|
20.0
|
1.0
|
CE2
|
C:TYR200
|
4.0
|
22.5
|
0.3
|
CH3
|
C:ACT406
|
4.1
|
21.2
|
0.7
|
CG
|
C:HIS226
|
4.2
|
22.6
|
1.0
|
ND1
|
C:HIS224
|
4.2
|
25.8
|
1.0
|
ND1
|
C:HIS226
|
4.3
|
22.1
|
1.0
|
CG
|
C:HIS224
|
4.4
|
20.8
|
1.0
|
O
|
C:HOH648
|
4.5
|
19.8
|
1.0
|
CE1
|
C:TYR200
|
4.7
|
19.6
|
0.3
|
CZ
|
C:ARG221
|
4.7
|
26.1
|
1.0
|
CD1
|
C:TYR164
|
4.9
|
22.5
|
1.0
|
CD
|
C:ARG221
|
5.0
|
26.5
|
1.0
|
|
Zinc binding site 4 out
of 8 in 9dr5
Go back to
Zinc Binding Sites List in 9dr5
Zinc binding site 4 out
of 8 in the Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form)
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 Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn401
b:23.4
occ:0.57
|
OH
|
D:TYR164
|
1.9
|
17.1
|
1.0
|
OXT
|
D:ACT404
|
1.9
|
21.7
|
0.6
|
NE2
|
D:HIS226
|
2.1
|
19.0
|
1.0
|
NE2
|
D:HIS224
|
2.2
|
21.5
|
1.0
|
OH
|
D:TYR200
|
2.5
|
15.2
|
0.4
|
C
|
D:ACT404
|
2.7
|
24.4
|
0.6
|
CD2
|
D:HIS226
|
2.9
|
20.6
|
1.0
|
O
|
D:ACT404
|
2.9
|
18.1
|
0.6
|
CZ
|
D:TYR164
|
2.9
|
16.0
|
1.0
|
CE1
|
D:HIS224
|
3.1
|
21.7
|
1.0
|
CE1
|
D:HIS226
|
3.3
|
20.3
|
1.0
|
CD2
|
D:HIS224
|
3.3
|
21.6
|
1.0
|
NH1
|
D:ARG221
|
3.6
|
29.5
|
1.0
|
CE1
|
D:TYR164
|
3.7
|
17.2
|
1.0
|
CE2
|
D:TYR164
|
3.8
|
14.6
|
1.0
|
CZ
|
D:TYR200
|
3.8
|
14.1
|
0.4
|
O
|
D:HOH543
|
4.0
|
17.3
|
1.0
|
CG
|
D:HIS226
|
4.1
|
15.4
|
1.0
|
CH3
|
D:ACT404
|
4.1
|
15.9
|
0.6
|
ND1
|
D:HIS224
|
4.2
|
20.4
|
1.0
|
ND1
|
D:HIS226
|
4.2
|
18.5
|
1.0
|
CE2
|
D:TYR200
|
4.3
|
16.6
|
0.4
|
CG
|
D:HIS224
|
4.3
|
17.9
|
1.0
|
O
|
D:HOH627
|
4.5
|
15.5
|
1.0
|
CZ
|
D:ARG221
|
4.7
|
23.8
|
1.0
|
CE1
|
D:TYR200
|
4.9
|
17.6
|
0.4
|
CD
|
D:ARG221
|
5.0
|
20.0
|
1.0
|
CD1
|
D:TYR164
|
5.0
|
17.0
|
1.0
|
|
Zinc binding site 5 out
of 8 in 9dr5
Go back to
Zinc Binding Sites List in 9dr5
Zinc binding site 5 out
of 8 in the Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form)
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 Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn401
b:24.7
occ:0.67
|
OXT
|
E:ACT404
|
1.8
|
23.7
|
0.7
|
OH
|
E:TYR164
|
1.8
|
18.4
|
1.0
|
NE2
|
E:HIS226
|
2.2
|
17.9
|
1.0
|
NE2
|
E:HIS224
|
2.3
|
23.6
|
1.0
|
OH
|
E:TYR200
|
2.5
|
20.3
|
0.3
|
C
|
E:ACT404
|
2.6
|
23.6
|
0.7
|
O
|
E:ACT404
|
2.9
|
19.9
|
0.7
|
CZ
|
E:TYR164
|
2.9
|
17.1
|
1.0
|
CD2
|
E:HIS226
|
3.0
|
18.0
|
1.0
|
CE1
|
E:HIS224
|
3.1
|
27.2
|
1.0
|
CE1
|
E:HIS226
|
3.3
|
18.8
|
1.0
|
CD2
|
E:HIS224
|
3.3
|
21.8
|
1.0
|
CE1
|
E:TYR164
|
3.6
|
16.1
|
1.0
|
NH1
|
E:ARG221
|
3.6
|
23.6
|
1.0
|
CZ
|
E:TYR200
|
3.7
|
18.0
|
0.3
|
CE2
|
E:TYR164
|
3.8
|
17.1
|
1.0
|
O
|
E:HOH520
|
3.9
|
16.2
|
1.0
|
CH3
|
E:ACT404
|
4.0
|
17.6
|
0.7
|
CE2
|
E:TYR200
|
4.1
|
20.6
|
0.3
|
CG
|
E:HIS226
|
4.2
|
14.9
|
1.0
|
ND1
|
E:HIS224
|
4.2
|
20.8
|
1.0
|
ND1
|
E:HIS226
|
4.3
|
15.3
|
1.0
|
CG
|
E:HIS224
|
4.4
|
17.2
|
1.0
|
O
|
E:HOH612
|
4.5
|
14.3
|
1.0
|
CZ
|
E:ARG221
|
4.7
|
24.5
|
1.0
|
CE1
|
E:TYR200
|
4.9
|
19.1
|
0.3
|
CD1
|
E:TYR164
|
4.9
|
17.0
|
1.0
|
CD
|
E:ARG221
|
5.0
|
22.5
|
1.0
|
|
Zinc binding site 6 out
of 8 in 9dr5
Go back to
Zinc Binding Sites List in 9dr5
Zinc binding site 6 out
of 8 in the Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form)
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 Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Zn401
b:28.4
occ:0.64
|
OH
|
F:TYR164
|
1.8
|
21.8
|
1.0
|
OXT
|
F:ACT406
|
1.8
|
26.9
|
0.6
|
NE2
|
F:HIS226
|
2.2
|
19.3
|
1.0
|
NE2
|
F:HIS224
|
2.2
|
23.2
|
1.0
|
OH
|
F:TYR200
|
2.5
|
20.3
|
0.4
|
C
|
F:ACT406
|
2.6
|
28.1
|
0.6
|
O
|
F:ACT406
|
2.8
|
22.3
|
0.6
|
CZ
|
F:TYR164
|
2.9
|
20.0
|
1.0
|
CD2
|
F:HIS226
|
3.0
|
23.2
|
1.0
|
CE1
|
F:HIS224
|
3.0
|
30.7
|
1.0
|
CE1
|
F:HIS226
|
3.3
|
22.9
|
1.0
|
CD2
|
F:HIS224
|
3.3
|
27.9
|
1.0
|
CE1
|
F:TYR164
|
3.5
|
21.3
|
1.0
|
NH1
|
F:ARG221
|
3.6
|
33.1
|
1.0
|
CZ
|
F:TYR200
|
3.7
|
22.9
|
0.4
|
CE2
|
F:TYR164
|
3.8
|
18.4
|
1.0
|
CH3
|
F:ACT406
|
4.0
|
24.1
|
0.6
|
O
|
F:HOH565
|
4.0
|
21.4
|
1.0
|
CE2
|
F:TYR200
|
4.1
|
19.9
|
0.4
|
CG
|
F:HIS226
|
4.2
|
18.6
|
1.0
|
ND1
|
F:HIS224
|
4.2
|
24.8
|
1.0
|
ND1
|
F:HIS226
|
4.3
|
21.5
|
1.0
|
CG
|
F:HIS224
|
4.4
|
24.4
|
1.0
|
O
|
F:HOH615
|
4.6
|
17.8
|
1.0
|
CZ
|
F:ARG221
|
4.7
|
33.6
|
1.0
|
CE1
|
F:TYR200
|
4.8
|
22.7
|
0.4
|
CD1
|
F:TYR164
|
4.8
|
22.5
|
1.0
|
CD
|
F:ARG221
|
5.0
|
23.2
|
1.0
|
CD1
|
F:LEU109
|
5.0
|
28.9
|
1.0
|
|
Zinc binding site 7 out
of 8 in 9dr5
Go back to
Zinc Binding Sites List in 9dr5
Zinc binding site 7 out
of 8 in the Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form)
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 Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Zn401
b:23.1
occ:0.55
|
OH
|
G:TYR164
|
1.8
|
17.5
|
1.0
|
OXT
|
G:ACT405
|
1.9
|
23.2
|
0.6
|
NE2
|
G:HIS226
|
2.2
|
20.6
|
1.0
|
NE2
|
G:HIS224
|
2.2
|
18.4
|
1.0
|
OH
|
G:TYR200
|
2.4
|
19.7
|
0.5
|
C
|
G:ACT405
|
2.6
|
20.6
|
0.6
|
O
|
G:ACT405
|
2.8
|
16.0
|
0.6
|
CZ
|
G:TYR164
|
2.9
|
20.0
|
1.0
|
CD2
|
G:HIS226
|
3.0
|
18.9
|
1.0
|
CE1
|
G:HIS224
|
3.1
|
22.9
|
1.0
|
CE1
|
G:HIS226
|
3.2
|
23.2
|
1.0
|
CD2
|
G:HIS224
|
3.3
|
21.7
|
1.0
|
NH1
|
G:ARG221
|
3.7
|
27.7
|
1.0
|
CZ
|
G:TYR200
|
3.7
|
18.3
|
0.5
|
CE1
|
G:TYR164
|
3.7
|
16.2
|
1.0
|
CE2
|
G:TYR164
|
3.8
|
18.0
|
1.0
|
O
|
G:HOH576
|
4.0
|
17.7
|
1.0
|
CH3
|
G:ACT405
|
4.1
|
18.9
|
0.6
|
CE1
|
G:TYR200
|
4.2
|
14.3
|
0.5
|
CG
|
G:HIS226
|
4.2
|
14.9
|
1.0
|
ND1
|
G:HIS224
|
4.2
|
18.4
|
1.0
|
ND1
|
G:HIS226
|
4.3
|
19.0
|
1.0
|
CG
|
G:HIS224
|
4.3
|
16.9
|
1.0
|
O
|
G:HOH628
|
4.6
|
16.3
|
1.0
|
CZ
|
G:ARG221
|
4.7
|
22.3
|
1.0
|
CE2
|
G:TYR200
|
4.8
|
20.2
|
0.5
|
CD
|
G:ARG221
|
4.9
|
18.8
|
1.0
|
CD1
|
G:TYR164
|
5.0
|
20.9
|
1.0
|
|
Zinc binding site 8 out
of 8 in 9dr5
Go back to
Zinc Binding Sites List in 9dr5
Zinc binding site 8 out
of 8 in the Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form)
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 Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Zn401
b:24.6
occ:0.59
|
OXT
|
H:ACT405
|
1.8
|
24.3
|
0.6
|
OH
|
H:TYR164
|
1.9
|
19.9
|
1.0
|
NE2
|
H:HIS226
|
2.2
|
19.4
|
1.0
|
NE2
|
H:HIS224
|
2.2
|
20.8
|
1.0
|
OH
|
H:TYR200
|
2.5
|
14.7
|
0.4
|
C
|
H:ACT405
|
2.6
|
24.9
|
0.6
|
O
|
H:ACT405
|
2.8
|
20.5
|
0.6
|
CZ
|
H:TYR164
|
2.9
|
17.5
|
1.0
|
CD2
|
H:HIS226
|
2.9
|
22.6
|
1.0
|
CE1
|
H:HIS224
|
3.1
|
26.5
|
1.0
|
CD2
|
H:HIS224
|
3.3
|
21.3
|
1.0
|
CE1
|
H:HIS226
|
3.3
|
23.5
|
1.0
|
CE1
|
H:TYR164
|
3.7
|
18.0
|
1.0
|
NH1
|
H:ARG221
|
3.7
|
22.9
|
1.0
|
CZ
|
H:TYR200
|
3.7
|
17.0
|
0.4
|
CE2
|
H:TYR164
|
3.8
|
17.8
|
1.0
|
O
|
H:HOH532
|
4.0
|
17.7
|
1.0
|
CH3
|
H:ACT405
|
4.0
|
17.9
|
0.6
|
CE2
|
H:TYR200
|
4.1
|
15.2
|
0.4
|
CG
|
H:HIS226
|
4.2
|
17.3
|
1.0
|
ND1
|
H:HIS224
|
4.3
|
19.7
|
1.0
|
ND1
|
H:HIS226
|
4.3
|
20.3
|
1.0
|
CG
|
H:HIS224
|
4.4
|
16.7
|
1.0
|
O
|
H:HOH566
|
4.6
|
15.6
|
1.0
|
CZ
|
H:ARG221
|
4.7
|
21.1
|
1.0
|
CE1
|
H:TYR200
|
4.8
|
19.4
|
0.4
|
CD1
|
H:TYR164
|
4.9
|
18.2
|
1.0
|
O
|
H:HOH501
|
5.0
|
26.6
|
1.0
|
|
Reference:
P.Enayati,
L.Liu,
S.Lovell,
G.W.Buchko,
K.P.Battaile.
Crystal Structure of Catechol 1,2-Dioxygenase From Burkholderia Multivorans (Zinc Bound, P1 Form) To Be Published.
Page generated: Thu Oct 31 15:26:07 2024
|