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Zinc in PDB 8yth: Crystal Structures of Human IRF2BP2 Ring Domain in Complex with ZBTB16 Peptide

Protein crystallography data

The structure of Crystal Structures of Human IRF2BP2 Ring Domain in Complex with ZBTB16 Peptide, PDB code: 8yth was solved by G.C.Wang, J.P.Ding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.37 / 2.40
Space group P 64
Cell size a, b, c (Å), α, β, γ (°) 47.315, 47.315, 57.489, 90, 90, 120
R / Rfree (%) 24.3 / 28.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structures of Human IRF2BP2 Ring Domain in Complex with ZBTB16 Peptide (pdb code 8yth). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structures of Human IRF2BP2 Ring Domain in Complex with ZBTB16 Peptide, PDB code: 8yth:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 8yth

Go back to Zinc Binding Sites List in 8yth
Zinc binding site 1 out of 3 in the Crystal Structures of Human IRF2BP2 Ring Domain in Complex with ZBTB16 Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structures of Human IRF2BP2 Ring Domain in Complex with ZBTB16 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:61.4
occ:1.00
SG A:CYS533 2.3 63.6 1.0
SG A:CYS530 2.3 55.4 1.0
SG A:CYS509 2.3 57.8 1.0
SG A:CYS506 2.4 50.2 1.0
CB A:CYS509 3.0 36.6 1.0
CB A:CYS506 3.2 46.4 1.0
CB A:CYS533 3.2 63.8 1.0
N A:CYS509 3.5 51.3 1.0
CB A:CYS530 3.6 52.6 1.0
CA A:CYS509 3.8 53.5 1.0
N A:CYS530 4.0 42.4 1.0
N A:CYS533 4.3 57.2 1.0
CA A:CYS533 4.4 59.0 1.0
CA A:CYS530 4.4 48.4 1.0
C A:CYS509 4.5 48.5 1.0
CB A:LEU508 4.6 56.5 1.0
N A:HIS510 4.6 47.5 1.0
CA A:CYS506 4.6 47.6 1.0
C A:LEU508 4.6 49.1 1.0
O A:CYS530 5.0 39.8 1.0
CA A:LEU508 5.0 54.0 1.0

Zinc binding site 2 out of 3 in 8yth

Go back to Zinc Binding Sites List in 8yth
Zinc binding site 2 out of 3 in the Crystal Structures of Human IRF2BP2 Ring Domain in Complex with ZBTB16 Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structures of Human IRF2BP2 Ring Domain in Complex with ZBTB16 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn602

b:48.3
occ:1.00
ND1 A:HIS527 2.1 56.9 1.0
SG A:CYS555 2.3 65.9 1.0
SG A:CYS549 2.3 53.3 1.0
SG A:CYS521 2.3 51.0 1.0
CE1 A:HIS527 2.9 57.7 1.0
CG A:HIS527 3.2 46.3 1.0
CB A:CYS555 3.2 71.5 1.0
CB A:CYS521 3.3 48.5 1.0
CB A:CYS549 3.4 50.2 1.0
CB A:HIS527 3.6 43.9 1.0
NE2 A:HIS527 4.1 48.6 1.0
CG2 A:VAL524 4.1 53.6 1.0
CB A:VAL524 4.1 51.9 1.0
CD2 A:HIS527 4.2 50.8 1.0
CB A:SER551 4.2 59.7 1.0
NE1 A:TRP564 4.3 57.7 1.0
CA A:CYS555 4.5 70.4 1.0
CA A:CYS521 4.6 46.4 1.0
N A:CYS555 4.7 65.9 1.0
CA A:CYS549 4.7 54.6 1.0
N A:VAL524 4.8 57.9 1.0
CZ A:PHE529 4.9 57.6 1.0
OG A:SER523 4.9 60.1 1.0

Zinc binding site 3 out of 3 in 8yth

Go back to Zinc Binding Sites List in 8yth
Zinc binding site 3 out of 3 in the Crystal Structures of Human IRF2BP2 Ring Domain in Complex with ZBTB16 Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structures of Human IRF2BP2 Ring Domain in Complex with ZBTB16 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn603

b:43.6
occ:1.00
SG A:CYS505 2.3 55.4 1.0
ND1 A:HIS510 2.3 38.4 1.0
CE1 A:HIS510 3.2 40.8 1.0
CG A:HIS510 3.3 45.6 1.0
O A:CYS506 3.5 45.0 1.0
CB A:HIS510 3.6 46.2 1.0
CA A:HIS510 3.8 53.2 1.0
CB A:CYS505 4.0 58.9 1.0
O A:CYS505 4.3 41.3 1.0
C A:CYS505 4.3 44.9 1.0
C A:CYS506 4.3 43.2 1.0
NE2 A:HIS510 4.4 43.2 1.0
O A:HOH701 4.4 29.9 1.0
CD2 A:HIS510 4.4 43.5 1.0
N A:CYS506 4.6 46.7 1.0
C A:HIS510 4.7 56.2 1.0
CA A:CYS505 4.7 57.3 1.0
N A:HIS510 4.8 47.5 1.0
CA A:THR507 4.8 42.7 1.0
O A:HIS510 4.9 54.0 1.0

Reference:

G.C.Wang, J.P.Ding. IRF2BP2 Recognizes and Bind to A Conserved Rxsvi Sequence Motif of Protein Partners and Interacts with ZBTB16 to Regulate Megakaryocytic Differentiation To Be Published.
Page generated: Wed Nov 27 21:08:10 2024

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