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Zinc in PDB 5td5: Crystal Structure of Human APOBEC3B Variant Complexed with Ssdna

Protein crystallography data

The structure of Crystal Structure of Human APOBEC3B Variant Complexed with Ssdna, PDB code: 5td5 was solved by K.Shi, S.Banerjee, K.Kurahashi, H.Aihara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 83.49 / 1.72
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 96.411, 96.411, 84.875, 90.00, 90.00, 120.00
R / Rfree (%) 18 / 20.9

Other elements in 5td5:

The structure of Crystal Structure of Human APOBEC3B Variant Complexed with Ssdna also contains other interesting chemical elements:

Iodine (I) 9 atoms
Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human APOBEC3B Variant Complexed with Ssdna (pdb code 5td5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human APOBEC3B Variant Complexed with Ssdna, PDB code: 5td5:

Zinc binding site 1 out of 1 in 5td5

Go back to Zinc Binding Sites List in 5td5
Zinc binding site 1 out of 1 in the Crystal Structure of Human APOBEC3B Variant Complexed with Ssdna


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 Human APOBEC3B Variant Complexed with Ssdna within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:23.7
occ:1.00
ND1 A:HIS253 2.1 29.9 1.0
SG A:CYS289 2.1 45.6 1.0
CL A:CL417 2.2 38.4 1.0
SG A:CYS284 2.3 34.1 1.0
HB2 A:CYS289 2.7 44.7 1.0
CB A:CYS289 2.9 37.2 1.0
CE1 A:HIS253 3.0 30.9 1.0
CG A:HIS253 3.1 32.0 1.0
HE1 A:HIS253 3.1 37.1 1.0
HB2 A:HIS253 3.2 35.1 1.0
HB3 A:CYS284 3.2 30.6 1.0
H A:CYS284 3.2 32.7 1.0
CB A:CYS284 3.4 25.5 1.0
HB3 A:CYS289 3.4 44.7 1.0
HB2 A:TRP287 3.4 43.6 1.0
CB A:HIS253 3.5 29.2 1.0
HB3 A:HIS253 3.5 35.1 1.0
H A:CYS289 3.7 43.0 1.0
H21 A:EDO411 3.7 62.2 1.0
N A:CYS284 3.9 27.3 1.0
HO2 A:EDO411 4.1 46.6 1.0
NE2 A:HIS253 4.1 35.0 1.0
HB2 A:CYS284 4.1 30.6 1.0
CA A:CYS284 4.1 27.1 1.0
H22 A:EDO411 4.1 62.2 1.0
CD2 A:HIS253 4.2 32.6 1.0
CA A:CYS289 4.2 41.9 1.0
N A:CYS289 4.3 35.9 1.0
C2 A:EDO411 4.3 51.8 1.0
CB A:TRP287 4.3 36.4 1.0
HE3 A:TRP287 4.5 45.9 1.0
HB3 A:TRP287 4.5 43.6 1.0
O A:CYS284 4.5 27.2 1.0
C A:CYS284 4.5 28.2 1.0
H A:TRP287 4.6 35.7 1.0
O2 A:EDO411 4.7 38.8 1.0
HA A:CYS289 4.7 50.3 1.0
HG A:LEU256 4.8 47.1 1.0
HA A:PRO283 4.9 31.0 1.0
HE2 A:HIS253 4.9 42.0 1.0
C4 C:DC0 4.9 22.9 1.0
N3 C:DC0 4.9 23.1 1.0
O C:HOH203 4.9 28.5 1.0
H A:HIS253 4.9 40.2 1.0
C A:TRP287 5.0 40.1 1.0
CA A:HIS253 5.0 29.5 1.0

Reference:

K.Shi, M.A.Carpenter, S.Banerjee, N.M.Shaban, K.Kurahashi, D.J.Salamango, J.L.Mccann, G.J.Starrett, J.V.Duffy, O.Demir, R.E.Amaro, D.A.Harki, R.S.Harris, H.Aihara. Structural Basis For Targeted Dna Cytosine Deamination and Mutagenesis By APOBEC3A and APOBEC3B. Nat. Struct. Mol. Biol. V. 24 131 2017.
ISSN: ESSN 1545-9985
PubMed: 27991903
DOI: 10.1038/NSMB.3344
Page generated: Mon Oct 28 08:26:08 2024

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