Zinc in PDB 6h3c: Cryo-Em Structure of the Brisc Complex Bound to SHMT2
Enzymatic activity of Cryo-Em Structure of the Brisc Complex Bound to SHMT2
All present enzymatic activity of Cryo-Em Structure of the Brisc Complex Bound to SHMT2:
2.1.2.1;
Zinc Binding Sites:
The binding sites of Zinc atom in the Cryo-Em Structure of the Brisc Complex Bound to SHMT2
(pdb code 6h3c). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Cryo-Em Structure of the Brisc Complex Bound to SHMT2, PDB code: 6h3c:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 6h3c
Go back to
Zinc Binding Sites List in 6h3c
Zinc binding site 1 out
of 2 in the Cryo-Em Structure of the Brisc Complex Bound to SHMT2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Cryo-Em Structure of the Brisc Complex Bound to SHMT2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn401
b:61.1
occ:1.00
|
OD2
|
B:ASP135
|
2.0
|
60.2
|
1.0
|
O
|
B:HOH1000
|
2.0
|
62.1
|
1.0
|
OD1
|
B:ASP135
|
2.1
|
60.2
|
1.0
|
NE2
|
B:HIS122
|
2.2
|
86.0
|
1.0
|
NE2
|
B:HIS124
|
2.3
|
47.9
|
1.0
|
CG
|
B:ASP135
|
2.4
|
60.2
|
1.0
|
H1
|
B:HOH1000
|
2.6
|
62.1
|
1.0
|
H2
|
B:HOH1000
|
2.6
|
62.1
|
1.0
|
CD2
|
B:HIS122
|
3.1
|
86.0
|
1.0
|
HD2
|
B:HIS122
|
3.1
|
86.0
|
1.0
|
CE1
|
B:HIS124
|
3.2
|
47.9
|
1.0
|
CE1
|
B:HIS122
|
3.3
|
86.0
|
1.0
|
HE1
|
B:HIS124
|
3.3
|
47.9
|
1.0
|
CD2
|
B:HIS124
|
3.3
|
47.9
|
1.0
|
HG21
|
B:VAL90
|
3.5
|
69.2
|
1.0
|
HE1
|
B:HIS122
|
3.5
|
86.0
|
1.0
|
HD2
|
B:HIS124
|
3.5
|
47.9
|
1.0
|
HD13
|
B:ILE153
|
3.7
|
51.4
|
1.0
|
H
|
B:SER132
|
3.7
|
56.1
|
1.0
|
CB
|
B:ASP135
|
3.8
|
60.2
|
1.0
|
HG
|
B:SER132
|
4.0
|
56.1
|
1.0
|
OG
|
B:SER132
|
4.1
|
56.1
|
1.0
|
HB3
|
B:ASP135
|
4.1
|
60.2
|
1.0
|
CG
|
B:HIS122
|
4.2
|
86.0
|
1.0
|
HB2
|
B:ASP135
|
4.2
|
60.2
|
1.0
|
HG22
|
B:VAL90
|
4.2
|
69.2
|
1.0
|
HB3
|
B:SER132
|
4.2
|
56.1
|
1.0
|
CG2
|
B:VAL90
|
4.3
|
69.2
|
1.0
|
ND1
|
B:HIS122
|
4.3
|
86.0
|
1.0
|
HA
|
B:PRO131
|
4.3
|
48.3
|
1.0
|
ND1
|
B:HIS124
|
4.3
|
47.9
|
1.0
|
OD1
|
B:ASP88
|
4.3
|
75.8
|
1.0
|
HD11
|
B:ILE153
|
4.4
|
51.4
|
1.0
|
HG12
|
B:ILE153
|
4.4
|
51.4
|
1.0
|
CD1
|
B:ILE153
|
4.4
|
51.4
|
1.0
|
CG
|
B:HIS124
|
4.4
|
47.9
|
1.0
|
HG23
|
B:VAL90
|
4.6
|
69.2
|
1.0
|
N
|
B:SER132
|
4.6
|
56.1
|
1.0
|
CB
|
B:SER132
|
4.7
|
56.1
|
1.0
|
HG21
|
B:ILE153
|
4.8
|
51.4
|
1.0
|
HA
|
B:ASP135
|
4.8
|
60.2
|
1.0
|
H
|
B:ASP135
|
4.8
|
60.2
|
1.0
|
HA
|
B:ASP88
|
4.8
|
75.8
|
1.0
|
CA
|
B:ASP135
|
4.8
|
60.2
|
1.0
|
HG2
|
B:GLU33
|
4.9
|
59.8
|
1.0
|
CG1
|
B:ILE153
|
5.0
|
51.4
|
1.0
|
HG11
|
B:VAL90
|
5.0
|
69.2
|
1.0
|
|
Zinc binding site 2 out
of 2 in 6h3c
Go back to
Zinc Binding Sites List in 6h3c
Zinc binding site 2 out
of 2 in the Cryo-Em Structure of the Brisc Complex Bound to SHMT2
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Cryo-Em Structure of the Brisc Complex Bound to SHMT2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Zn401
b:65.0
occ:1.00
|
OD2
|
G:ASP135
|
2.0
|
60.5
|
1.0
|
O
|
G:HOH1000
|
2.0
|
61.8
|
1.0
|
OD1
|
G:ASP135
|
2.1
|
60.5
|
1.0
|
NE2
|
G:HIS122
|
2.2
|
86.0
|
1.0
|
NE2
|
G:HIS124
|
2.3
|
45.2
|
1.0
|
CG
|
G:ASP135
|
2.4
|
60.5
|
1.0
|
H1
|
G:HOH1000
|
2.6
|
61.8
|
1.0
|
H2
|
G:HOH1000
|
2.6
|
61.8
|
1.0
|
CD2
|
G:HIS122
|
3.1
|
86.0
|
1.0
|
HD2
|
G:HIS122
|
3.2
|
86.0
|
1.0
|
CE1
|
G:HIS124
|
3.2
|
45.2
|
1.0
|
CE1
|
G:HIS122
|
3.3
|
86.0
|
1.0
|
HE1
|
G:HIS124
|
3.3
|
45.2
|
1.0
|
CD2
|
G:HIS124
|
3.3
|
45.2
|
1.0
|
HG21
|
G:VAL90
|
3.5
|
69.6
|
1.0
|
HE1
|
G:HIS122
|
3.5
|
86.0
|
1.0
|
HD2
|
G:HIS124
|
3.5
|
45.2
|
1.0
|
HD13
|
G:ILE153
|
3.7
|
50.3
|
1.0
|
H
|
G:SER132
|
3.7
|
56.1
|
1.0
|
CB
|
G:ASP135
|
3.8
|
60.5
|
1.0
|
HG
|
G:SER132
|
4.0
|
56.1
|
1.0
|
OG
|
G:SER132
|
4.1
|
56.1
|
1.0
|
HB3
|
G:ASP135
|
4.1
|
60.5
|
1.0
|
CG
|
G:HIS122
|
4.2
|
86.0
|
1.0
|
HB2
|
G:ASP135
|
4.2
|
60.5
|
1.0
|
HG22
|
G:VAL90
|
4.2
|
69.6
|
1.0
|
HB3
|
G:SER132
|
4.2
|
56.1
|
1.0
|
CG2
|
G:VAL90
|
4.3
|
69.6
|
1.0
|
ND1
|
G:HIS122
|
4.3
|
86.0
|
1.0
|
HA
|
G:PRO131
|
4.3
|
47.4
|
1.0
|
ND1
|
G:HIS124
|
4.3
|
45.2
|
1.0
|
OD1
|
G:ASP88
|
4.3
|
75.2
|
1.0
|
HD11
|
G:ILE153
|
4.4
|
50.3
|
1.0
|
HG12
|
G:ILE153
|
4.4
|
50.3
|
1.0
|
CD1
|
G:ILE153
|
4.4
|
50.3
|
1.0
|
CG
|
G:HIS124
|
4.4
|
45.2
|
1.0
|
HG23
|
G:VAL90
|
4.6
|
69.6
|
1.0
|
N
|
G:SER132
|
4.6
|
56.1
|
1.0
|
CB
|
G:SER132
|
4.7
|
56.1
|
1.0
|
HG21
|
G:ILE153
|
4.8
|
50.3
|
1.0
|
HA
|
G:ASP135
|
4.8
|
60.5
|
1.0
|
H
|
G:ASP135
|
4.8
|
60.5
|
1.0
|
HA
|
G:ASP88
|
4.8
|
75.2
|
1.0
|
CA
|
G:ASP135
|
4.8
|
60.5
|
1.0
|
HG2
|
G:GLU33
|
4.9
|
59.2
|
1.0
|
CG1
|
G:ILE153
|
5.0
|
50.3
|
1.0
|
HG11
|
G:VAL90
|
5.0
|
69.6
|
1.0
|
|
Reference:
J.Rabl,
R.D.Bunker,
A.D.Schenk,
S.Cavadini,
M.E.Gill,
W.Abdulrahman,
A.Andres-Pons,
M.S.Luijsterburg,
A.F.M.Ibrahim,
E.Branigan,
J.D.Aguirre,
A.H.Marceau,
C.Guerillon,
T.Bouwmeester,
U.Hassiepen,
A.H.F.M.Peters,
M.Renatus,
L.Gelman,
S.M.Rubin,
N.Mailand,
H.Van Attikum,
R.T.Hay,
N.H.Thoma.
Structural Basis of BRCC36 Function in Dna Repair and Immune Regulation. Mol.Cell V. 75 483 2019.
ISSN: ISSN 1097-2765
PubMed: 31253574
DOI: 10.1016/J.MOLCEL.2019.06.002
Page generated: Mon Oct 28 22:21:35 2024
|