Atomistry » Zinc » PDB 5cvi-5d7w » 5d1m
Atomistry »
  Zinc »
    PDB 5cvi-5d7w »
      5d1m »

Zinc in PDB 5d1m: Crystal Structure of UBCH5B in Complex with the Ring-U5BR Fragment of AO7 (P199A)

Enzymatic activity of Crystal Structure of UBCH5B in Complex with the Ring-U5BR Fragment of AO7 (P199A)

All present enzymatic activity of Crystal Structure of UBCH5B in Complex with the Ring-U5BR Fragment of AO7 (P199A):
6.3.2.19;

Protein crystallography data

The structure of Crystal Structure of UBCH5B in Complex with the Ring-U5BR Fragment of AO7 (P199A), PDB code: 5d1m was solved by Y.-H.Liang, S.Li, A.M.Weissman, X.Ji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.40 / 1.58
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 105.696, 47.415, 67.975, 90.00, 118.32, 90.00
R / Rfree (%) 18.8 / 22.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of UBCH5B in Complex with the Ring-U5BR Fragment of AO7 (P199A) (pdb code 5d1m). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of UBCH5B in Complex with the Ring-U5BR Fragment of AO7 (P199A), PDB code: 5d1m:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5d1m

Go back to Zinc Binding Sites List in 5d1m
Zinc binding site 1 out of 2 in the Crystal Structure of UBCH5B in Complex with the Ring-U5BR Fragment of AO7 (P199A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of UBCH5B in Complex with the Ring-U5BR Fragment of AO7 (P199A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:19.6
occ:1.00
SG B:CYS138 2.3 19.1 1.0
ND1 B:HIS158 2.3 18.9 1.0
SG B:CYS135 2.4 16.7 1.0
SG B:CYS161 2.4 19.1 1.0
CB B:CYS135 3.0 17.2 1.0
CB B:CYS138 3.2 19.4 1.0
CG B:HIS158 3.3 18.7 1.0
CE1 B:HIS158 3.3 23.1 1.0
CB B:CYS161 3.4 17.4 1.0
CB B:HIS158 3.5 16.3 1.0
N B:CYS138 3.8 16.9 1.0
N B:HIS158 3.9 16.5 1.0
CA B:CYS138 4.1 15.3 1.0
CA B:HIS158 4.3 17.2 1.0
NE2 B:HIS158 4.4 21.3 1.0
CD2 B:HIS158 4.4 19.9 1.0
CA B:CYS135 4.5 15.7 1.0
O B:CYS135 4.7 20.4 1.0
CA B:CYS161 4.8 16.2 1.0
C B:CYS135 4.8 16.8 1.0
NE2 B:GLN220 4.9 33.3 1.0
C B:ILE137 4.9 18.0 1.0
CB B:ILE137 4.9 16.2 1.0

Zinc binding site 2 out of 2 in 5d1m

Go back to Zinc Binding Sites List in 5d1m
Zinc binding site 2 out of 2 in the Crystal Structure of UBCH5B in Complex with the Ring-U5BR Fragment of AO7 (P199A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of UBCH5B in Complex with the Ring-U5BR Fragment of AO7 (P199A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn302

b:18.2
occ:1.00
ND1 B:HIS155 2.2 19.6 1.0
SG B:CYS198 2.3 16.8 1.0
SG B:CYS153 2.3 16.4 1.0
SG B:CYS201 2.4 17.1 1.0
CE1 B:HIS155 2.9 18.9 1.0
CB B:CYS198 3.2 15.7 1.0
CB B:CYS153 3.4 16.4 1.0
CG B:HIS155 3.4 15.8 1.0
CB B:CYS201 3.7 15.4 1.0
N B:CYS201 3.9 16.1 1.0
CB B:HIS155 4.0 16.0 1.0
NE2 B:HIS155 4.1 22.1 1.0
O B:CYS153 4.2 16.5 1.0
CB B:VAL200 4.3 17.0 1.0
OG1 B:THR151 4.3 15.5 1.0
CA B:CYS201 4.3 17.3 1.0
CD2 B:HIS155 4.4 20.0 1.0
C B:CYS153 4.5 16.5 1.0
CA B:CYS153 4.5 16.4 1.0
CA B:CYS198 4.7 17.9 1.0
CG1 B:VAL200 4.8 18.3 1.0
O B:HOH429 4.8 21.5 0.5
C B:VAL200 4.8 20.9 1.0
CA B:VAL200 4.9 19.3 1.0
N B:VAL200 4.9 18.9 1.0
CB B:GLU203 5.0 18.2 0.3
O B:HOH401 5.0 29.1 1.0

Reference:

S.Li, Y.H.Liang, J.Mariano, M.B.Metzger, D.K.Stringer, V.A.Hristova, J.Li, P.A.Randazzo, Y.C.Tsai, X.Ji, A.M.Weissman. Insights Into Ubiquitination From the Unique Clamp-Like Binding of the Ring E3 AO7 to the E2 UBCH5B. J.Biol.Chem. V. 290 30225 2015.
ISSN: ESSN 1083-351X
PubMed: 26475854
DOI: 10.1074/JBC.M115.685867
Page generated: Sun Oct 27 14:35:27 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy