Zinc in PDB 7mju: Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail

Protein crystallography data

The structure of Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail, PDB code: 7mju was solved by B.J.Klein, T.G.Kutateladze, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.08 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.92, 54.33, 47.78, 90, 106.82, 90
R / Rfree (%) 16.5 / 20.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail (pdb code 7mju). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail, PDB code: 7mju:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in 7mju

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Zinc binding site 1 out of 5 in the Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail


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 AF10 Pzp Bound to Histone H3 Tail within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:22.4
occ:1.00
ND1 A:HIS52 2.1 24.5 1.0
SG A:CYS55 2.3 22.5 1.0
SG A:CYS28 2.3 22.8 1.0
SG A:CYS25 2.3 20.1 1.0
CB A:CYS25 3.0 19.3 1.0
CE1 A:HIS52 3.0 24.4 1.0
CG A:HIS52 3.1 24.2 1.0
CB A:CYS28 3.2 24.4 1.0
CB A:CYS55 3.2 18.7 1.0
CB A:HIS52 3.4 24.3 1.0
N A:CYS28 3.8 27.5 1.0
N A:HIS52 4.0 19.3 1.0
O A:HOH540 4.0 44.8 1.0
CA A:CYS28 4.1 24.4 1.0
NE2 A:HIS52 4.2 30.6 1.0
O A:HOH473 4.2 36.4 1.0
CD2 A:HIS52 4.2 25.7 1.0
CA A:HIS52 4.3 21.1 1.0
CA A:CYS25 4.5 25.9 1.0
CB A:VAL27 4.6 20.9 1.0
CA A:CYS55 4.7 23.0 1.0
C A:CYS28 4.8 25.7 1.0
C A:VAL27 4.8 25.4 1.0
N A:SER29 5.0 23.1 1.0

Zinc binding site 2 out of 5 in 7mju

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Zinc binding site 2 out of 5 in the Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail


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 Human AF10 Pzp Bound to Histone H3 Tail within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:28.1
occ:1.00
SG A:CYS47 2.3 27.9 1.0
SG A:CYS42 2.4 26.5 1.0
SG A:CYS71 2.4 30.8 1.0
SG A:CYS68 2.4 23.2 1.0
CB A:CYS47 3.2 27.5 1.0
CB A:CYS42 3.3 25.6 1.0
CB A:CYS68 3.4 22.3 1.0
CB A:CYS71 3.4 32.4 1.0
N A:CYS68 3.9 23.5 1.0
O A:HOH546 4.1 53.2 1.0
CA A:CYS68 4.2 23.0 1.0
N A:CYS71 4.2 30.1 1.0
CA A:CYS71 4.4 33.5 1.0
CB A:VAL49 4.4 24.5 1.0
CA A:CYS47 4.6 29.9 1.0
CG2 A:VAL49 4.6 26.0 1.0
CA A:GLY44 4.6 27.0 1.0
N A:GLY44 4.6 33.5 1.0
CA A:CYS42 4.7 22.6 1.0
C A:CYS68 4.7 21.0 1.0
O A:CYS68 4.8 24.4 1.0

Zinc binding site 3 out of 5 in 7mju

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Zinc binding site 3 out of 5 in the Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn303

b:26.2
occ:1.00
ND1 A:HIS167 2.1 25.1 1.0
SG A:CYS137 2.3 26.5 1.0
SG A:CYS140 2.3 27.7 1.0
SG A:CYS170 2.4 25.5 1.0
CE1 A:HIS167 3.0 20.2 1.0
CB A:CYS137 3.1 23.8 1.0
CG A:HIS167 3.2 20.5 1.0
CB A:CYS140 3.3 26.6 1.0
CB A:CYS170 3.5 26.7 1.0
CB A:HIS167 3.5 18.1 1.0
N A:CYS140 3.8 24.8 1.0
CA A:CYS140 4.0 28.1 1.0
N A:HIS167 4.1 20.1 1.0
NE2 A:HIS167 4.2 22.5 1.0
CD2 A:HIS167 4.3 19.0 1.0
NH2 A:ARG145 4.4 38.2 1.0
CG A:PRO86 4.4 27.1 1.0
CA A:HIS167 4.4 21.0 1.0
CD A:PRO86 4.5 25.6 1.0
NE A:ARG145 4.5 32.7 1.0
CA A:CYS137 4.6 26.1 1.0
CB A:ILE139 4.8 29.6 1.0
CA A:CYS170 4.9 19.9 1.0
C A:ILE139 4.9 31.5 1.0
CZ A:ARG145 5.0 37.7 1.0

Zinc binding site 4 out of 5 in 7mju

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Zinc binding site 4 out of 5 in the Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn304

b:23.5
occ:1.00
ND1 A:HIS102 2.1 22.8 1.0
SG A:CYS82 2.2 20.4 1.0
SG A:CYS105 2.3 20.0 1.0
SG A:CYS85 2.4 19.6 1.0
CE1 A:HIS102 3.0 17.8 1.0
CB A:CYS82 3.0 18.0 1.0
CG A:HIS102 3.1 22.7 1.0
CB A:CYS85 3.1 13.7 1.0
CB A:HIS102 3.5 14.3 1.0
CB A:CYS105 3.5 21.3 1.0
N A:CYS85 3.8 20.3 1.0
CG2 A:THR169 3.9 16.9 1.0
CA A:CYS85 4.0 24.1 1.0
N A:HIS102 4.0 19.5 1.0
NE2 A:HIS102 4.1 23.6 1.0
CD2 A:HIS102 4.2 17.8 1.0
C A:LEU84 4.3 28.8 1.0
CA A:HIS102 4.4 23.6 1.0
OG1 A:THR169 4.4 27.4 1.0
CB A:LEU84 4.5 18.7 1.0
CA A:CYS82 4.5 24.3 1.0
C A:CYS85 4.6 29.7 1.0
O A:HIS87 4.7 33.2 1.0
O A:CYS85 4.7 26.4 1.0
N A:LEU84 4.7 19.4 1.0
CA A:LEU84 4.8 25.4 1.0
CB A:THR169 4.8 20.7 1.0
CA A:CYS105 4.8 20.4 1.0
O A:HOH464 4.9 23.8 1.0
O A:LEU84 5.0 22.6 1.0

Zinc binding site 5 out of 5 in 7mju

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Zinc binding site 5 out of 5 in the Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Human AF10 Pzp Bound to Histone H3 Tail within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn305

b:28.7
occ:1.00
ND1 A:HIS197 2.0 29.9 1.0
SG A:CYS162 2.3 27.0 1.0
SG A:CYS157 2.4 25.3 1.0
SG A:CYS194 2.4 26.9 1.0
CE1 A:HIS197 3.0 28.2 1.0
CB A:CYS157 3.0 19.3 1.0
CG A:HIS197 3.1 27.6 1.0
CB A:CYS162 3.2 22.7 1.0
CB A:CYS194 3.4 23.3 1.0
CB A:HIS197 3.5 29.9 1.0
N A:CYS194 3.9 23.6 1.0
NE2 A:HIS197 4.1 29.6 1.0
CD2 A:HIS197 4.2 30.3 1.0
CA A:CYS194 4.2 23.3 1.0
CB A:LYS159 4.3 25.8 1.0
CB A:GLN164 4.4 28.4 1.0
CG A:GLN164 4.5 33.4 1.0
CA A:CYS157 4.5 26.0 1.0
N A:HIS197 4.6 34.6 1.0
CA A:CYS162 4.6 27.8 1.0
CA A:HIS197 4.7 32.4 1.0
O A:CYS194 4.8 20.4 1.0
C A:CYS194 4.8 23.9 1.0

Reference:

B.J.Klein, A.Deshpande, K.L.Cox, F.Xuan, M.Zandian, K.Barbosa, S.Khanal, Q.Tong, Y.Zhang, P.Zhang, A.Sinha, S.K.Bohlander, X.Shi, H.Wen, M.G.Poirier, A.J.Deshpande, T.G.Kutateladze. The Role of the Pzp Domain of AF10 in Acute Leukemia Driven By AF10 Translocations. Nat Commun V. 12 4130 2021.
ISSN: ESSN 2041-1723
PubMed: 34226546
DOI: 10.1038/S41467-021-24418-9
Page generated: Sun Aug 22 09:48:33 2021

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