Iron in PDB 6scg: Structure of Adhe Form 1
Enzymatic activity of Structure of Adhe Form 1
All present enzymatic activity of Structure of Adhe Form 1:
1.1.1.1;
1.2.1.10;
Protein crystallography data
The structure of Structure of Adhe Form 1, PDB code: 6scg
was solved by
A.L.Lovering,
E.Bragginton,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.02 /
1.65
|
Space group
|
P 43 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
97.138,
97.138,
233.432,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
15.5 /
18.1
|
Iron Binding Sites:
The binding sites of Iron atom in the Structure of Adhe Form 1
(pdb code 6scg). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Structure of Adhe Form 1, PDB code: 6scg:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 6scg
Go back to
Iron Binding Sites List in 6scg
Iron binding site 1 out
of 2 in the Structure of Adhe Form 1
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Structure of Adhe Form 1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe905
b:23.0
occ:1.00
|
NE2
|
A:HIS737
|
2.1
|
24.4
|
1.0
|
OD1
|
A:ASP653
|
2.1
|
24.2
|
1.0
|
NE2
|
A:HIS657
|
2.1
|
18.9
|
1.0
|
NE2
|
A:HIS723
|
2.2
|
23.2
|
1.0
|
O
|
A:HOH1218
|
2.2
|
34.5
|
1.0
|
O
|
A:HOH1005
|
2.3
|
28.0
|
1.0
|
CD2
|
A:HIS737
|
3.0
|
27.8
|
1.0
|
CG
|
A:ASP653
|
3.0
|
23.2
|
1.0
|
CD2
|
A:HIS723
|
3.0
|
23.4
|
1.0
|
CE1
|
A:HIS657
|
3.0
|
20.7
|
1.0
|
CD2
|
A:HIS657
|
3.1
|
19.1
|
1.0
|
OD2
|
A:ASP653
|
3.2
|
23.6
|
1.0
|
CE1
|
A:HIS737
|
3.2
|
28.5
|
1.0
|
CE1
|
A:HIS723
|
3.2
|
24.3
|
1.0
|
OD1
|
A:ASN741
|
3.9
|
33.8
|
1.0
|
ND1
|
A:HIS657
|
4.1
|
19.7
|
1.0
|
CG
|
A:HIS737
|
4.2
|
27.5
|
1.0
|
CG
|
A:HIS657
|
4.2
|
18.5
|
1.0
|
ND1
|
A:HIS737
|
4.2
|
30.0
|
1.0
|
CG
|
A:HIS723
|
4.2
|
22.7
|
1.0
|
ND1
|
A:HIS723
|
4.3
|
23.4
|
1.0
|
CB
|
A:ASP653
|
4.5
|
22.1
|
1.0
|
O
|
A:HOH1002
|
4.5
|
52.5
|
1.0
|
C4N
|
A:NAD901
|
4.6
|
54.9
|
0.6
|
O
|
A:HOH1151
|
4.7
|
32.8
|
1.0
|
O
|
A:ASP653
|
4.7
|
19.1
|
1.0
|
C5N
|
A:NAD901
|
4.8
|
50.3
|
0.6
|
CG
|
A:ASN741
|
4.9
|
26.3
|
1.0
|
CA
|
A:ASP653
|
4.9
|
20.7
|
1.0
|
|
Iron binding site 2 out
of 2 in 6scg
Go back to
Iron Binding Sites List in 6scg
Iron binding site 2 out
of 2 in the Structure of Adhe Form 1
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Structure of Adhe Form 1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe904
b:17.3
occ:1.00
|
NE2
|
B:HIS737
|
2.1
|
17.9
|
1.0
|
NE2
|
B:HIS657
|
2.1
|
15.2
|
1.0
|
OD1
|
B:ASP653
|
2.1
|
18.3
|
1.0
|
NE2
|
B:HIS723
|
2.2
|
18.0
|
1.0
|
O
|
B:HOH1262
|
2.3
|
24.1
|
1.0
|
O
|
B:HOH1010
|
2.3
|
24.0
|
1.0
|
CD2
|
B:HIS737
|
3.0
|
18.6
|
1.0
|
CG
|
B:ASP653
|
3.0
|
16.3
|
1.0
|
CD2
|
B:HIS723
|
3.0
|
17.4
|
1.0
|
CE1
|
B:HIS657
|
3.1
|
15.8
|
1.0
|
CD2
|
B:HIS657
|
3.1
|
14.6
|
1.0
|
CE1
|
B:HIS737
|
3.1
|
21.1
|
1.0
|
OD2
|
B:ASP653
|
3.2
|
18.3
|
1.0
|
CE1
|
B:HIS723
|
3.2
|
17.7
|
1.0
|
OD1
|
B:ASN741
|
3.9
|
25.8
|
1.0
|
ND1
|
B:HIS657
|
4.2
|
14.9
|
1.0
|
CG
|
B:HIS737
|
4.2
|
19.9
|
1.0
|
CG
|
B:HIS657
|
4.2
|
14.5
|
1.0
|
ND1
|
B:HIS737
|
4.2
|
21.3
|
1.0
|
CG
|
B:HIS723
|
4.2
|
17.5
|
1.0
|
ND1
|
B:HIS723
|
4.3
|
17.3
|
1.0
|
O
|
B:HOH1193
|
4.3
|
31.9
|
1.0
|
CB
|
B:ASP653
|
4.5
|
15.8
|
1.0
|
O
|
B:ASP653
|
4.8
|
15.2
|
1.0
|
CG
|
B:ASN741
|
4.9
|
18.9
|
1.0
|
CA
|
B:ASP653
|
5.0
|
16.2
|
1.0
|
|
Reference:
A.L.Lovering,
A.L.Lovering,
E.Bragginton.
N/A N/A.
Page generated: Wed Aug 7 09:36:34 2024
|