Zinc in PDB 1su3: X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action
Enzymatic activity of X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action
All present enzymatic activity of X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action:
3.4.24.7;
Protein crystallography data
The structure of X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action, PDB code: 1su3
was solved by
D.Jozic,
G.Bourenkov,
N.H.Lim,
H.Nagase,
W.Bode,
K.Maskos,
Structural Proteomics In Europe (Spine),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
2.20
|
Space group
|
I 4 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
142.746,
142.746,
295.308,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
22.3 /
25.2
|
Other elements in 1su3:
The structure of X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action
(pdb code 1su3). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action, PDB code: 1su3:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 1su3
Go back to
Zinc Binding Sites List in 1su3
Zinc binding site 1 out
of 4 in the X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn913
b:34.8
occ:1.00
|
NE2
|
A:HIS222
|
2.0
|
31.5
|
1.0
|
NE2
|
A:HIS228
|
2.0
|
33.8
|
1.0
|
NE2
|
A:HIS218
|
2.0
|
31.2
|
1.0
|
SG
|
A:CYS92
|
2.2
|
27.4
|
1.0
|
CD2
|
A:HIS228
|
2.9
|
31.4
|
1.0
|
CE1
|
A:HIS222
|
2.9
|
33.8
|
1.0
|
CB
|
A:CYS92
|
3.0
|
29.1
|
1.0
|
CD2
|
A:HIS222
|
3.0
|
34.2
|
1.0
|
CD2
|
A:HIS218
|
3.0
|
30.2
|
1.0
|
CE1
|
A:HIS218
|
3.0
|
31.5
|
1.0
|
CE1
|
A:HIS228
|
3.1
|
35.5
|
1.0
|
CB
|
A:VAL94
|
4.0
|
29.8
|
1.0
|
ND1
|
A:HIS222
|
4.1
|
32.5
|
1.0
|
CG
|
A:HIS228
|
4.1
|
33.2
|
1.0
|
CG
|
A:HIS222
|
4.1
|
33.7
|
1.0
|
ND1
|
A:HIS228
|
4.1
|
32.4
|
1.0
|
ND1
|
A:HIS218
|
4.1
|
27.3
|
1.0
|
CG
|
A:HIS218
|
4.1
|
28.8
|
1.0
|
CG2
|
A:VAL94
|
4.3
|
29.6
|
1.0
|
CA
|
A:CYS92
|
4.4
|
28.7
|
1.0
|
N
|
A:VAL94
|
4.7
|
29.6
|
1.0
|
CE
|
A:MET236
|
4.7
|
32.3
|
1.0
|
CG1
|
A:VAL94
|
4.9
|
29.9
|
1.0
|
CA
|
A:VAL94
|
4.9
|
30.1
|
1.0
|
O
|
A:VAL94
|
4.9
|
30.5
|
1.0
|
C
|
A:CYS92
|
4.9
|
29.1
|
1.0
|
|
Zinc binding site 2 out
of 4 in 1su3
Go back to
Zinc Binding Sites List in 1su3
Zinc binding site 2 out
of 4 in the X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn915
b:42.3
occ:1.00
|
ND1
|
A:HIS196
|
1.8
|
31.6
|
1.0
|
OD2
|
A:ASP170
|
2.0
|
43.6
|
1.0
|
NE2
|
A:HIS183
|
2.1
|
36.3
|
1.0
|
NE2
|
A:HIS168
|
2.1
|
39.7
|
1.0
|
CE1
|
A:HIS196
|
2.7
|
35.0
|
1.0
|
CG
|
A:HIS196
|
2.9
|
35.1
|
1.0
|
CD2
|
A:HIS168
|
2.9
|
39.8
|
1.0
|
CG
|
A:ASP170
|
2.9
|
42.8
|
1.0
|
CE1
|
A:HIS183
|
3.0
|
36.0
|
1.0
|
CD2
|
A:HIS183
|
3.1
|
32.8
|
1.0
|
OD1
|
A:ASP170
|
3.1
|
39.9
|
1.0
|
CE1
|
A:HIS168
|
3.2
|
38.8
|
1.0
|
CB
|
A:HIS196
|
3.4
|
33.9
|
1.0
|
NE2
|
A:HIS196
|
3.8
|
34.4
|
1.0
|
CD2
|
A:HIS196
|
4.0
|
36.2
|
1.0
|
O
|
A:SER172
|
4.0
|
44.3
|
1.0
|
CG
|
A:HIS168
|
4.1
|
41.5
|
1.0
|
ND1
|
A:HIS183
|
4.1
|
35.6
|
1.0
|
ND1
|
A:HIS168
|
4.2
|
41.1
|
1.0
|
CG
|
A:HIS183
|
4.2
|
34.1
|
1.0
|
CE1
|
A:PHE185
|
4.3
|
41.1
|
1.0
|
CB
|
A:ASP170
|
4.3
|
44.9
|
1.0
|
CZ
|
A:PHE185
|
4.5
|
41.4
|
1.0
|
CE2
|
A:PHE174
|
4.7
|
35.6
|
1.0
|
CB
|
A:SER172
|
4.8
|
45.8
|
1.0
|
CZ
|
A:PHE174
|
4.8
|
36.8
|
1.0
|
O
|
A:HOH978
|
4.9
|
49.4
|
1.0
|
CA
|
A:HIS196
|
4.9
|
34.1
|
1.0
|
CG2
|
A:VAL164
|
4.9
|
36.7
|
1.0
|
|
Zinc binding site 3 out
of 4 in 1su3
Go back to
Zinc Binding Sites List in 1su3
Zinc binding site 3 out
of 4 in the X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn913
b:35.6
occ:1.00
|
NE2
|
B:HIS228
|
1.9
|
35.0
|
1.0
|
NE2
|
B:HIS218
|
2.0
|
33.9
|
1.0
|
NE2
|
B:HIS222
|
2.0
|
34.9
|
1.0
|
SG
|
B:CYS92
|
2.3
|
40.0
|
1.0
|
CE1
|
B:HIS228
|
2.9
|
34.1
|
1.0
|
CD2
|
B:HIS228
|
2.9
|
32.7
|
1.0
|
CB
|
B:CYS92
|
2.9
|
39.8
|
1.0
|
CD2
|
B:HIS222
|
2.9
|
37.1
|
1.0
|
CE1
|
B:HIS218
|
3.0
|
35.6
|
1.0
|
CD2
|
B:HIS218
|
3.0
|
33.5
|
1.0
|
CE1
|
B:HIS222
|
3.1
|
37.0
|
1.0
|
CB
|
B:VAL94
|
3.9
|
39.5
|
1.0
|
ND1
|
B:HIS228
|
4.0
|
32.5
|
1.0
|
CG
|
B:HIS228
|
4.0
|
33.8
|
1.0
|
ND1
|
B:HIS218
|
4.1
|
35.1
|
1.0
|
CG
|
B:HIS222
|
4.1
|
35.6
|
1.0
|
CG
|
B:HIS218
|
4.1
|
33.9
|
1.0
|
ND1
|
B:HIS222
|
4.1
|
37.8
|
1.0
|
CG2
|
B:VAL94
|
4.2
|
41.0
|
1.0
|
CA
|
B:CYS92
|
4.4
|
40.0
|
1.0
|
CE
|
B:MET236
|
4.7
|
35.2
|
1.0
|
CG1
|
B:VAL94
|
4.8
|
38.7
|
1.0
|
N
|
B:VAL94
|
4.8
|
38.7
|
1.0
|
C
|
B:CYS92
|
4.8
|
39.8
|
1.0
|
CA
|
B:VAL94
|
4.9
|
39.4
|
1.0
|
|
Zinc binding site 4 out
of 4 in 1su3
Go back to
Zinc Binding Sites List in 1su3
Zinc binding site 4 out
of 4 in the X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of X-Ray Structure of Human Prommp-1: New Insights Into Collagenase Action within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn915
b:45.7
occ:1.00
|
OD2
|
B:ASP170
|
1.7
|
43.2
|
1.0
|
ND1
|
B:HIS196
|
1.9
|
36.3
|
1.0
|
NE2
|
B:HIS183
|
2.1
|
41.5
|
1.0
|
NE2
|
B:HIS168
|
2.2
|
41.2
|
1.0
|
CG
|
B:ASP170
|
2.8
|
46.0
|
1.0
|
CE1
|
B:HIS196
|
2.8
|
39.9
|
1.0
|
CD2
|
B:HIS168
|
2.9
|
41.8
|
1.0
|
CE1
|
B:HIS183
|
3.0
|
41.8
|
1.0
|
CG
|
B:HIS196
|
3.0
|
37.6
|
1.0
|
CD2
|
B:HIS183
|
3.1
|
39.9
|
1.0
|
OD1
|
B:ASP170
|
3.2
|
41.0
|
1.0
|
CE1
|
B:HIS168
|
3.4
|
42.6
|
1.0
|
CB
|
B:HIS196
|
3.4
|
36.6
|
1.0
|
NE2
|
B:HIS196
|
3.9
|
40.4
|
1.0
|
O
|
B:SER172
|
4.0
|
46.6
|
1.0
|
CD2
|
B:HIS196
|
4.1
|
39.6
|
1.0
|
CB
|
B:ASP170
|
4.1
|
47.4
|
1.0
|
ND1
|
B:HIS183
|
4.1
|
41.6
|
1.0
|
CG
|
B:HIS168
|
4.2
|
43.6
|
1.0
|
CG
|
B:HIS183
|
4.2
|
39.6
|
1.0
|
CE1
|
B:PHE185
|
4.3
|
42.0
|
1.0
|
ND1
|
B:HIS168
|
4.3
|
41.6
|
1.0
|
CZ
|
B:PHE185
|
4.5
|
41.9
|
1.0
|
CE2
|
B:PHE174
|
4.7
|
39.6
|
1.0
|
CB
|
B:SER172
|
4.7
|
47.6
|
1.0
|
CZ
|
B:PHE174
|
4.8
|
39.5
|
1.0
|
CG2
|
B:VAL164
|
4.9
|
40.3
|
1.0
|
O
|
B:HOH946
|
4.9
|
50.2
|
1.0
|
CA
|
B:HIS196
|
4.9
|
36.5
|
1.0
|
C
|
B:SER172
|
5.0
|
46.9
|
1.0
|
|
Reference:
D.Jozic,
G.Bourenkov,
N.H.Lim,
R.Visse,
H.Nagase,
W.Bode,
K.Maskos.
X-Ray Structure of Human Prommp-1: New Insights Into Procollagenase Activation and Collagen Binding. J.Biol.Chem. V. 280 9578 2005.
ISSN: ISSN 0021-9258
PubMed: 15611040
DOI: 10.1074/JBC.M411084200
Page generated: Wed Oct 16 18:55:37 2024
|