Zinc in PDB 8tau: Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb

Enzymatic activity of Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb

All present enzymatic activity of Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb:
2.3.2.23; 2.3.2.24;

Zinc Binding Sites:

The binding sites of Zinc atom in the Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb (pdb code 8tau). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb, PDB code: 8tau:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 8tau

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Zinc binding site 1 out of 4 in the Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn101

b:261.5
occ:1.00
H C:CYS26 3.3 239.3 1.0
H C:HIS56 3.7 234.3 1.0
N C:CYS26 3.9 239.3 1.0
O C:CYS23 3.9 240.5 1.0
H C:MET28 4.1 238.6 1.0
H C:ILE25 4.4 234.8 1.0
C C:CYS23 4.4 240.5 1.0
HA C:CYS34 4.4 243.8 1.0
CA C:CYS26 4.5 239.3 1.0
CA C:CYS23 4.5 240.5 1.0
N C:HIS56 4.6 234.3 1.0
C C:ILE25 4.7 234.8 1.0
H C:ARG27 4.8 237.5 1.0
N C:ILE25 4.9 234.8 1.0
N C:MET28 4.9 238.6 1.0
CA C:ILE25 5.0 234.8 1.0
HA C:CYS23 5.0 240.5 1.0

Zinc binding site 2 out of 4 in 8tau

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Zinc binding site 2 out of 4 in the Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn102

b:265.6
occ:1.00
HA C:CYS44 2.6 237.1 1.0
CA C:CYS44 3.2 237.1 1.0
H C:CYS34 3.9 243.8 1.0
O C:ASP43 3.9 235.3 1.0
N C:CYS44 4.1 237.1 1.0
C C:CYS44 4.3 237.1 1.0
C C:ASP43 4.3 235.3 1.0
H C:HIS58 4.6 234.2 1.0
N C:CYS34 4.6 243.8 1.0
O C:CYS44 4.6 237.1 1.0
H C:CYS37 4.6 239.7 1.0
N C:CYS37 4.7 239.7 1.0
CA C:CYS34 4.8 243.8 1.0
H C:CYS44 4.8 237.1 1.0
CA C:CYS37 4.8 239.7 1.0

Zinc binding site 3 out of 4 in 8tau

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Zinc binding site 3 out of 4 in the Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn103

b:261.2
occ:1.00
O C:CYS51 2.3 229.5 1.0
C C:CYS51 3.4 229.5 1.0
HA C:CYS51 3.7 229.5 1.0
CA C:CYS51 3.9 229.5 1.0
CA C:CYS76 4.1 234.9 1.0
H C:CYS76 4.2 234.9 1.0
N C:CYS76 4.2 234.9 1.0
N C:SER52 4.5 229.5 1.0
HA C:CYS76 4.7 234.9 1.0
C C:MET75 4.7 233.8 1.0
C C:SER52 4.7 229.5 1.0
N C:HIS53 4.9 233.2 1.0
CA C:SER52 4.9 229.5 1.0
H C:HIS53 5.0 233.2 1.0

Zinc binding site 4 out of 4 in 8tau

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Zinc binding site 4 out of 4 in the Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Apc/C-CDH1-UBE2C-UBE2S-Ubiquitin-Cyclinb within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Zn901

b:206.7
occ:1.00
HA N:CYS231 2.6 176.8 1.0
H N:TRP232 2.8 169.9 1.0
CA N:CYS231 3.2 176.8 1.0
H N:CYS233 3.2 168.9 1.0
N N:TRP232 3.4 169.9 1.0
C N:CYS231 3.7 176.8 1.0
N N:CYS233 3.8 168.9 1.0
H N:GLY223 3.8 175.9 1.0
CA N:CYS233 4.2 168.9 1.0
HA N:CYS233 4.4 168.9 1.0
N N:CYS231 4.4 176.8 1.0
CA N:TRP232 4.6 169.9 1.0
C N:TRP232 4.6 169.9 1.0
N N:GLY223 4.6 175.9 1.0
N N:CYS224 4.6 182.5 1.0
H N:ALA222 4.7 173.5 1.0
H N:CYS224 4.7 182.5 1.0
CA N:CYS221 4.8 183.1 1.0
O N:CYS231 4.8 176.8 1.0
C N:GLY223 4.8 175.9 1.0
H N:CYS231 4.8 176.8 1.0
C N:CYS221 4.9 183.1 1.0
N N:ALA222 4.9 173.5 1.0
CA N:CYS224 4.9 182.5 1.0

Reference:

T.Bodrug, K.A.Welsh, D.L.Bolhuis, E.Paulakonis, R.C.Martinez-Chacin, B.Liu, N.Pinkin, T.Bonacci, L.Cui, P.Xu, O.Roscow, S.J.Amann, I.Grishkovskaya, M.J.Emanuele, J.S.Harrison, J.P.Steimel, K.M.Hahn, W.Zhang, E.D.Zhong, D.Haselbach, N.G.Brown. Time-Resolved Cryo-Em (Tr-Em) Analysis of Substrate Polyubiquitination By the Ring E3 Anaphase-Promoting Complex/Cyclosome (Apc/C) Nat.Struct.Mol.Biol. 2023.
ISSN: ESSN 1545-9985
DOI: 10.1038/S41594-023-01105-5
Page generated: Thu Oct 31 11:29:42 2024

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