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Manganese in PDB 5fpv: Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A

Enzymatic activity of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A

All present enzymatic activity of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A:
1.14.11.27;

Protein crystallography data

The structure of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A, PDB code: 5fpv was solved by V.Srikannathasan, C.Gileadi, F.Von Delft, C.H.Arrowsmith, C.Bountra, A.Edwards, U.Oppermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 85.327 / 2.44
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 111.346, 103.509, 157.103, 90.00, 106.37, 90.00
R / Rfree (%) 19.55 / 22.89

Other elements in 5fpv:

The structure of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A also contains other interesting chemical elements:

Nickel (Ni) 15 atoms
Zinc (Zn) 8 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A (pdb code 5fpv). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 8 binding sites of Manganese where determined in the Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A, PDB code: 5fpv:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Manganese binding site 1 out of 8 in 5fpv

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Manganese binding site 1 out of 8 in the Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1357

b:20.9
occ:1.00
O A:HOH2094 2.0 19.2 1.0
OE2 A:GLU191 2.1 21.6 1.0
NE2 A:HIS189 2.1 26.3 1.0
NAR A:MMK1358 2.2 19.3 1.0
NE2 A:HIS277 2.2 21.5 1.0
N A:MMK1358 2.3 18.6 1.0
CE1 A:HIS189 2.9 25.4 1.0
CAL A:MMK1358 3.0 18.8 1.0
CAM A:MMK1358 3.0 20.7 1.0
CE1 A:HIS277 3.1 21.4 1.0
CD A:GLU191 3.1 23.3 1.0
CA A:MMK1358 3.1 21.8 1.0
CAQ A:MMK1358 3.2 16.6 1.0
CD2 A:HIS189 3.2 26.3 1.0
CD2 A:HIS277 3.3 21.0 1.0
OE1 A:GLU191 3.5 24.4 1.0
ND1 A:HIS189 4.1 24.0 1.0
ND1 A:HIS277 4.3 20.0 1.0
CG A:HIS189 4.3 24.4 1.0
CAN A:MMK1358 4.4 20.9 1.0
CG A:HIS277 4.4 20.1 1.0
CG A:GLU191 4.4 21.9 1.0
CAP A:MMK1358 4.5 21.2 1.0
C A:MMK1358 4.5 26.8 1.0
OG A:SER197 4.5 23.2 1.0
O A:HOH2099 4.6 30.9 1.0
O A:MMK1358 4.8 27.0 1.0
CAO A:MMK1358 5.0 20.9 1.0

Manganese binding site 2 out of 8 in 5fpv

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Manganese binding site 2 out of 8 in the Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1357

b:17.9
occ:1.00
OE2 B:GLU191 2.0 26.1 1.0
NE2 B:HIS189 2.1 24.4 1.0
NAR B:MMK1358 2.2 20.4 1.0
O B:HOH2095 2.2 25.7 1.0
N B:MMK1358 2.2 18.0 1.0
NE2 B:HIS277 2.3 22.8 1.0
CE1 B:HIS189 3.0 18.0 1.0
CAL B:MMK1358 3.0 17.9 1.0
CAM B:MMK1358 3.0 22.1 1.0
CD B:GLU191 3.0 24.3 1.0
CE1 B:HIS277 3.1 21.3 1.0
CAQ B:MMK1358 3.1 19.2 1.0
CA B:MMK1358 3.2 27.0 1.0
CD2 B:HIS189 3.3 24.6 1.0
CD2 B:HIS277 3.3 21.6 1.0
OE1 B:GLU191 3.4 24.2 1.0
ND1 B:HIS189 4.2 24.4 1.0
ND1 B:HIS277 4.3 20.5 1.0
CG B:HIS189 4.3 24.0 1.0
CG B:GLU191 4.3 22.7 1.0
CAN B:MMK1358 4.4 22.9 1.0
CG B:HIS277 4.4 21.1 1.0
CAP B:MMK1358 4.4 21.2 1.0
C B:MMK1358 4.4 27.7 1.0
OG B:SER197 4.5 25.5 1.0
O B:MMK1358 4.7 27.2 1.0
CAO B:MMK1358 4.9 23.3 1.0

Manganese binding site 3 out of 8 in 5fpv

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Manganese binding site 3 out of 8 in the Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn1357

b:23.7
occ:1.00
NAR C:MMK1358 2.0 18.8 1.0
OE2 C:GLU191 2.1 29.5 1.0
NE2 C:HIS189 2.2 32.6 1.0
NE2 C:HIS277 2.3 30.0 1.0
O C:HOH2103 2.3 21.4 1.0
N C:MMK1358 2.3 33.7 1.0
CAM C:MMK1358 2.9 25.9 1.0
CAL C:MMK1358 3.0 30.2 1.0
CE1 C:HIS189 3.0 32.4 1.0
CAQ C:MMK1358 3.0 18.6 1.0
CD C:GLU191 3.1 27.9 1.0
CE1 C:HIS277 3.1 29.3 1.0
CA C:MMK1358 3.1 34.6 1.0
CD2 C:HIS189 3.3 33.4 1.0
CD2 C:HIS277 3.4 29.3 1.0
OE1 C:GLU191 3.5 27.9 1.0
ND1 C:HIS189 4.2 32.4 1.0
CAN C:MMK1358 4.2 22.9 1.0
ND1 C:HIS277 4.3 28.2 1.0
CAP C:MMK1358 4.3 21.3 1.0
CG C:HIS189 4.4 33.2 1.0
CG C:GLU191 4.4 25.0 1.0
CG C:HIS277 4.4 27.8 1.0
OG C:SER197 4.4 24.6 1.0
C C:MMK1358 4.6 37.5 1.0
CAO C:MMK1358 4.8 22.7 1.0
CB C:SER197 5.0 21.8 1.0

Manganese binding site 4 out of 8 in 5fpv

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Manganese binding site 4 out of 8 in the Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn1357

b:18.7
occ:1.00
OE2 D:GLU191 2.0 24.9 1.0
NAR D:MMK1358 2.1 21.1 1.0
NE2 D:HIS189 2.1 27.1 1.0
O D:HOH2089 2.2 18.9 1.0
NE2 D:HIS277 2.2 20.0 1.0
N D:MMK1358 2.4 26.4 1.0
CAM D:MMK1358 2.9 22.2 1.0
CE1 D:HIS189 2.9 26.7 1.0
CAL D:MMK1358 2.9 23.6 1.0
CE1 D:HIS277 3.0 20.2 1.0
CAQ D:MMK1358 3.1 20.6 1.0
CD D:GLU191 3.1 24.1 1.0
CD2 D:HIS189 3.2 28.2 1.0
CA D:MMK1358 3.2 29.8 1.0
CD2 D:HIS277 3.3 21.5 1.0
OE1 D:GLU191 3.6 22.0 1.0
ND1 D:HIS189 4.1 28.6 1.0
ND1 D:HIS277 4.2 21.4 1.0
O D:HOH2093 4.2 26.4 1.0
CAN D:MMK1358 4.2 22.9 1.0
CG D:HIS189 4.3 28.9 1.0
CG D:HIS277 4.3 22.0 1.0
CAP D:MMK1358 4.4 22.2 1.0
CG D:GLU191 4.4 23.5 1.0
OG D:SER197 4.6 22.4 1.0
C D:MMK1358 4.6 33.5 1.0
CAO D:MMK1358 4.8 25.6 1.0
O D:MMK1358 4.9 34.5 1.0

Manganese binding site 5 out of 8 in 5fpv

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Manganese binding site 5 out of 8 in the Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn1357

b:26.7
occ:1.00
OE2 E:GLU191 2.0 27.3 1.0
O E:HOH2057 2.1 24.3 1.0
NAR E:MMK1358 2.2 38.2 1.0
NE2 E:HIS277 2.2 24.8 1.0
NE2 E:HIS189 2.2 27.9 1.0
N E:MMK1358 2.5 39.0 1.0
CE1 E:HIS189 3.0 28.2 1.0
CD E:GLU191 3.1 27.2 1.0
CE1 E:HIS277 3.1 24.8 1.0
CAM E:MMK1358 3.1 37.5 1.0
CAQ E:MMK1358 3.1 37.2 1.0
CAL E:MMK1358 3.2 37.5 1.0
CA E:MMK1358 3.2 42.6 1.0
CD2 E:HIS277 3.3 25.8 1.0
CD2 E:HIS189 3.4 27.9 1.0
OE1 E:GLU191 3.5 27.4 1.0
ND1 E:HIS189 4.2 28.6 1.0
ND1 E:HIS277 4.2 24.9 1.0
CG E:GLU191 4.4 26.9 1.0
CG E:HIS277 4.4 26.2 1.0
CG E:HIS189 4.4 28.5 1.0
CAP E:MMK1358 4.4 36.8 1.0
CAN E:MMK1358 4.4 36.3 1.0
OG E:SER197 4.5 29.0 1.0
C E:MMK1358 4.6 47.0 1.0
CAO E:MMK1358 4.9 36.7 1.0

Manganese binding site 6 out of 8 in 5fpv

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Manganese binding site 6 out of 8 in the Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mn1357

b:27.6
occ:1.00
OE2 F:GLU191 2.1 33.3 1.0
O F:HOH2049 2.1 23.1 1.0
NE2 F:HIS189 2.1 31.1 1.0
NAR F:MMK1358 2.3 36.5 1.0
NE2 F:HIS277 2.3 27.2 1.0
N F:MMK1358 2.5 39.0 1.0
CE1 F:HIS189 2.9 30.6 1.0
CAL F:MMK1358 3.0 37.4 1.0
CAM F:MMK1358 3.0 37.4 1.0
CD F:GLU191 3.1 31.6 1.0
CE1 F:HIS277 3.1 28.2 1.0
CD2 F:HIS189 3.3 30.4 1.0
CAQ F:MMK1358 3.3 37.1 1.0
CD2 F:HIS277 3.3 26.6 1.0
CA F:MMK1358 3.4 43.0 1.0
OE1 F:GLU191 3.5 31.9 1.0
ND1 F:HIS189 4.1 30.1 1.0
ND1 F:HIS277 4.3 28.1 1.0
CG F:HIS189 4.3 29.1 1.0
CG F:HIS277 4.4 27.7 1.0
CAN F:MMK1358 4.4 37.7 1.0
CG F:GLU191 4.4 28.3 1.0
C F:MMK1358 4.4 46.4 1.0
O F:MMK1358 4.5 47.1 1.0
OG F:SER197 4.6 28.6 1.0
CAP F:MMK1358 4.6 37.9 1.0
O F:HOH2053 4.8 41.6 1.0

Manganese binding site 7 out of 8 in 5fpv

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Manganese binding site 7 out of 8 in the Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mn1357

b:23.6
occ:1.00
NAR G:MMK1358 1.9 26.7 1.0
OE2 G:GLU191 2.1 31.2 1.0
NE2 G:HIS189 2.1 25.6 1.0
O G:HOH2044 2.2 25.0 1.0
NE2 G:HIS277 2.2 28.9 1.0
N G:MMK1358 2.3 28.6 1.0
CAQ G:MMK1358 2.9 27.1 1.0
CAM G:MMK1358 2.9 27.1 1.0
CE1 G:HIS189 2.9 26.4 1.0
CAL G:MMK1358 3.0 26.8 1.0
CE1 G:HIS277 3.1 30.0 1.0
CD G:GLU191 3.1 31.8 1.0
CA G:MMK1358 3.2 31.4 1.0
CD2 G:HIS189 3.2 26.9 1.0
CD2 G:HIS277 3.3 27.8 1.0
OE1 G:GLU191 3.5 35.2 1.0
ND1 G:HIS189 4.1 27.8 1.0
CAP G:MMK1358 4.2 27.4 1.0
CAN G:MMK1358 4.2 28.0 1.0
ND1 G:HIS277 4.3 29.1 1.0
CG G:HIS189 4.3 28.1 1.0
CG G:HIS277 4.4 28.9 1.0
CG G:GLU191 4.4 31.4 1.0
C G:MMK1358 4.5 35.0 1.0
OG G:SER197 4.5 30.0 1.0
CAO G:MMK1358 4.7 30.1 1.0
O G:MMK1358 4.8 34.4 1.0

Manganese binding site 8 out of 8 in 5fpv

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Manganese binding site 8 out of 8 in the Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Crystal Structure of Human JMJD2A in Complex with Compound KDOAM20A within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mn1357

b:17.4
occ:1.00
NAR H:MMK1358 2.1 23.0 1.0
OE2 H:GLU191 2.1 25.1 1.0
NE2 H:HIS189 2.1 28.3 1.0
O H:HOH2075 2.1 18.5 1.0
NE2 H:HIS277 2.3 22.1 1.0
N H:MMK1358 2.3 24.8 1.0
CE1 H:HIS189 2.9 27.1 1.0
CAM H:MMK1358 3.0 22.5 1.0
CAQ H:MMK1358 3.0 24.1 1.0
CAL H:MMK1358 3.0 21.8 1.0
CA H:MMK1358 3.1 28.9 1.0
CE1 H:HIS277 3.1 23.1 1.0
CD H:GLU191 3.1 25.1 1.0
CD2 H:HIS189 3.2 28.1 1.0
CD2 H:HIS277 3.3 22.5 1.0
OE1 H:GLU191 3.6 26.1 1.0
ND1 H:HIS189 4.1 27.2 1.0
CG H:HIS189 4.3 27.3 1.0
ND1 H:HIS277 4.3 22.7 1.0
CAN H:MMK1358 4.3 23.1 1.0
CAP H:MMK1358 4.3 25.4 1.0
CG H:HIS277 4.4 22.4 1.0
CG H:GLU191 4.4 23.8 1.0
C H:MMK1358 4.5 33.6 1.0
OG H:SER197 4.6 22.2 1.0
CAO H:MMK1358 4.8 25.9 1.0
O H:MMK1358 4.9 34.4 1.0

Reference:

C.Johansson, S.Velupillai, A.Tumber, A.Szykowska, E.S.Hookway, R.P.Nowak, C.Strain-Damerell, C.Gileadi, M.Philpott, N.Burgess-Brown, N.Wu, J.Kopec, A.Nuzzi, H.Steuber, U.Egner, V.Badock, S.Munro, N.B.Lathangue, S.Westaway, J.Brown, N.Athanasou, R.Prinjha, P.E.Brennan, U.Oppermann. Structural Analysis of Human KDM5B Guides Histone Demethylase Inhibitor Development. Nat.Chem.Biol. V. 12 539 2016.
ISSN: ISSN 1552-4450
PubMed: 27214403
DOI: 10.1038/NCHEMBIO.2087
Page generated: Tue Dec 15 04:39:11 2020

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