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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

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