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Zinc in PDB 5fbj: Complex Structure of JMJD5 and Substrate

Enzymatic activity of Complex Structure of JMJD5 and Substrate

All present enzymatic activity of Complex Structure of JMJD5 and Substrate:
1.14.11.27;

Protein crystallography data

The structure of Complex Structure of JMJD5 and Substrate, PDB code: 5fbj was solved by H.L.Liu, Y.Wang, C.Wang, G.Y.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.98 / 2.42
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.539, 65.052, 77.950, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 24.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Complex Structure of JMJD5 and Substrate (pdb code 5fbj). 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 Complex Structure of JMJD5 and Substrate, PDB code: 5fbj:

Zinc binding site 1 out of 1 in 5fbj

Go back to Zinc Binding Sites List in 5fbj
Zinc binding site 1 out of 1 in the Complex Structure of JMJD5 and Substrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Complex Structure of JMJD5 and Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn503

b:24.3
occ:1.00
OD2 A:ASP323 2.0 19.7 1.0
O2 A:AKG501 2.1 18.8 1.0
O5 A:AKG501 2.3 19.0 1.0
NE2 A:HIS400 2.3 15.9 1.0
NE2 A:HIS321 2.3 17.4 1.0
C1 A:AKG501 2.8 18.0 1.0
C2 A:AKG501 2.9 19.0 1.0
CG A:ASP323 3.1 19.6 1.0
CD2 A:HIS400 3.2 15.8 1.0
CE1 A:HIS400 3.2 16.1 1.0
CD2 A:HIS321 3.3 17.8 1.0
CE1 A:HIS321 3.3 18.2 1.0
O A:NMM502 3.4 23.4 0.7
OD1 A:ASP323 3.5 21.0 1.0
OXT A:NMM502 3.6 23.3 0.6
C A:NMM502 4.0 22.0 0.5
O1 A:AKG501 4.0 21.4 1.0
CZ2 A:TRP414 4.3 21.6 1.0
ND1 A:HIS400 4.4 16.2 1.0
ND1 A:HIS321 4.4 18.3 1.0
CB A:ASP323 4.4 18.9 1.0
C3 A:AKG501 4.4 18.3 1.0
CG A:HIS400 4.4 15.2 1.0
CG A:HIS321 4.4 18.5 1.0
C4 A:AKG501 4.9 17.1 1.0
ND2 A:ASN327 4.9 16.5 1.0
NE1 A:TRP414 5.0 19.6 1.0

Reference:

H.L.Liu, Y.Wang, C.Wang, S.D.Dai, G.Y.Zhang. To Be Published To Be Published.
Page generated: Wed Dec 16 06:13:35 2020

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