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Zinc in PDB 5b78: Crystal Structure of Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14

Enzymatic activity of Crystal Structure of Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14

All present enzymatic activity of Crystal Structure of Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14:
2.3.1.48;

Protein crystallography data

The structure of Crystal Structure of Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14, PDB code: 5b78 was solved by H.Li, X.Xiong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.10 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.671, 48.238, 76.366, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 18.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14 (pdb code 5b78). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14, PDB code: 5b78:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 5b78

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Zinc binding site 1 out of 4 in the Crystal Structure of Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14


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 Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:21.2
occ:1.00
 SG A:CYS310 2.2 25.6 1.0
SG A:CYS284 2.3 18.6 1.0
SG A:CYS307 2.3 23.4 1.0
SG A:CYS281 2.3 20.7 1.0
CB A:CYS281 3.2 17.5 1.0
CB A:CYS284 3.4 22.0 1.0
CB A:CYS310 3.4 26.0 1.0
CB A:CYS307 3.5 21.2 1.0
N A:CYS284 3.8 20.1 1.0
N A:CYS307 4.0 23.6 1.0
N A:CYS310 4.0 32.2 1.0
CA A:CYS284 4.1 20.0 1.0
CA A:CYS307 4.3 22.1 1.0
CA A:CYS310 4.3 32.0 1.0
CB A:SER283 4.4 26.8 1.0
NH1 A:ARG286 4.6 22.1 1.0
CA A:CYS281 4.6 16.6 1.0
C A:SER283 4.6 23.4 1.0
C A:CYS307 4.8 28.0 1.0
OG A:SER283 4.8 34.9 1.0
C A:CYS284 4.8 16.9 1.0
CB A:ILE309 4.9 30.1 1.0
O A:CYS307 4.9 28.0 1.0
CA A:SER283 4.9 23.2 1.0
N A:SER283 4.9 24.0 1.0
O A:HOH531 5.0 36.5 1.0
C A:ILE309 5.0 31.5 1.0
N A:ASP285 5.0 15.0 1.0

Zinc binding site 2 out of 4 in 5b78

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Zinc binding site 2 out of 4 in the Crystal Structure of Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14


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 Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:18.5
occ:1.00
 ND1 A:HIS289 2.1 20.2 1.0
SG A:CYS292 2.3 20.6 1.0
SG A:CYS268 2.3 20.7 1.0
SG A:CYS265 2.3 16.2 1.0
CB A:CYS265 3.0 16.8 1.0
CE1 A:HIS289 3.1 18.2 1.0
CG A:HIS289 3.1 15.7 1.0
CB A:CYS292 3.2 17.1 1.0
CB A:CYS268 3.3 22.6 1.0
CB A:HIS289 3.5 17.3 1.0
N A:CYS268 3.8 19.6 1.0
O A:HOH666 4.0 35.2 1.0
N A:HIS289 4.1 14.7 1.0
CA A:CYS268 4.1 20.6 1.0
NE2 A:HIS289 4.2 17.9 1.0
CD2 A:HIS289 4.2 21.4 1.0
CA A:HIS289 4.4 15.3 1.0
CA A:CYS265 4.5 14.4 1.0
CA A:CYS292 4.6 18.2 1.0
O A:HOH504 4.7 38.4 1.0
CB A:SER267 4.7 20.1 1.0
C A:CYS268 4.9 22.6 1.0
C A:SER267 4.9 22.9 1.0
N A:CYS292 5.0 17.3 1.0

Zinc binding site 3 out of 4 in 5b78

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Zinc binding site 3 out of 4 in the Crystal Structure of Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14


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 Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:12.8
occ:1.00
 ND1 A:HIS238 2.1 12.3 1.0
SG A:CYS241 2.3 13.7 1.0
SG A:CYS212 2.3 13.5 1.0
SG A:CYS209 2.4 12.6 1.0
CE1 A:HIS238 3.0 13.2 1.0
CB A:CYS209 3.1 12.2 1.0
CG A:HIS238 3.2 13.1 1.0
CB A:CYS212 3.3 12.0 1.0
CB A:CYS241 3.4 12.3 1.0
CB A:HIS238 3.5 12.9 1.0
N A:CYS212 3.7 12.3 1.0
CA A:CYS212 4.0 12.4 1.0
N A:HIS238 4.1 12.9 1.0
NE2 A:HIS238 4.2 15.0 1.0
CD2 A:HIS238 4.3 15.1 1.0
O A:HOH527 4.3 18.1 1.0
CA A:HIS238 4.4 13.4 1.0
CA A:CYS209 4.6 11.0 1.0
CA A:CYS241 4.7 13.3 1.0
CB A:PHE211 4.7 12.1 1.0
C A:CYS212 4.8 14.3 1.0
C A:PHE211 4.8 12.9 1.0
N A:LEU213 4.9 13.9 1.0
N A:CYS241 4.9 13.2 1.0
CA A:ASN219 5.0 18.2 1.0
N A:GLY214 5.0 14.3 1.0

Zinc binding site 4 out of 4 in 5b78

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Zinc binding site 4 out of 4 in the Crystal Structure of Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14


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 Moz Double Phd Finger Mutant-S210D/N235R in Complex with Histone H3 Crotonylation at K14 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn404

b:11.5
occ:1.00
 SG A:CYS233 2.3 12.1 1.0
SG A:CYS259 2.3 11.0 1.0
SG A:CYS230 2.3 11.4 1.0
SG A:CYS262 2.4 12.0 1.0
CB A:CYS262 3.2 12.5 1.0
CB A:CYS230 3.2 10.9 1.0
CB A:CYS233 3.3 13.2 1.0
CB A:CYS259 3.4 12.1 1.0
N A:CYS233 3.7 11.0 1.0
N A:CYS259 4.0 11.3 1.0
CA A:CYS233 4.1 12.1 1.0
N A:CYS262 4.2 12.5 1.0
CA A:CYS259 4.3 9.9 1.0
CA A:CYS262 4.3 11.7 1.0
O B:HOH107 4.6 22.0 1.0
CA A:CYS230 4.6 10.9 1.0
C A:ASP232 4.7 13.8 1.0
CB A:ASP232 4.8 14.7 1.0
C A:CYS233 4.9 11.9 1.0
C A:CYS259 4.9 10.7 1.0

Reference:

X.Xiong, T.Panchenko, S.Yang, S.Zhao, P.Yan, W.Zhang, W.Xie, Y.Li, Y.Zhao, C.D.Allis, H.Li. Selective Recognition of Histone Crotonylation By Double Phd Fingers of Moz and DPF2 Nat.Chem.Biol. V. 12 1111 2016.
ISSN: ESSN 1552-4469
PubMed: 27775714
DOI: 10.1038/NCHEMBIO.2218
Page generated: Sun Oct 27 13:26:24 2024

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