Iron in PDB 6jzz: The Crystal Structure of Aar-C294S in Complex with Ado.

All present enzymatic activity of The Crystal Structure of Aar-C294S in Complex with Ado.:
1.2.1.80; 4.1.99.5;

The structure of The Crystal Structure of Aar-C294S in Complex with Ado., PDB code: 6jzz was solved by H.M.Zhang, M.Li, Y.Gao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.66 / 3.01
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	66.527, 72.335, 137.196, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 26.9

The binding sites of Iron atom in the The Crystal Structure of Aar-C294S in Complex with Ado. (pdb code 6jzz). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The Crystal Structure of Aar-C294S in Complex with Ado., PDB code: 6jzz:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the The Crystal Structure of Aar-C294S in Complex with Ado.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Crystal Structure of Aar-C294S in Complex with Ado. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:53.0 occ:1.00 OE1 B:GLU32 2.3 56.3 1.0 OE2 B:GLU60 2.4 63.9 1.0 OE2 B:GLU32 2.4 54.7 1.0 ND1 B:HIS63 2.6 63.7 1.0 OE1 B:GLU60 2.6 64.3 1.0 OE1 B:GLU144 2.7 60.2 1.0 CD B:GLU32 2.7 56.0 1.0 CD B:GLU60 2.8 64.3 1.0 FE B:FE2303 3.0 77.6 1.0 CD B:GLU144 3.1 60.3 1.0 OE2 B:GLU144 3.1 61.4 1.0 CE1 B:HIS63 3.4 64.0 1.0 CG B:HIS63 3.6 63.8 1.0 C1 B:PL3302 3.7 52.5 1.0 O1 B:PL3302 3.7 50.4 1.0 CB B:HIS63 3.9 67.2 1.0 CG B:GLU32 4.2 60.3 1.0 CG B:GLU60 4.2 70.1 1.0 CG B:GLU144 4.3 55.8 1.0 CA B:GLU60 4.5 73.3 1.0 OH B:TYR122 4.5 50.1 1.0 NE2 B:HIS63 4.6 66.4 1.0 CE1 B:HIS147 4.6 61.1 1.0 CG2 B:VAL140 4.6 59.0 1.0 CD2 B:HIS63 4.7 66.9 1.0 CB B:GLU60 4.7 71.4 1.0 CE2 B:TYR122 4.8 50.7 1.0 ND1 B:HIS147 4.8 59.8 1.0 CB B:GLU32 5.0 63.9 1.0

Iron binding site 2 out of 2 in the The Crystal Structure of Aar-C294S in Complex with Ado.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Crystal Structure of Aar-C294S in Complex with Ado. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe303 b:77.6 occ:1.00 OE2 B:GLU144 2.4 61.4 1.0 ND1 B:HIS147 2.5 59.8 1.0 OE1 B:GLU60 2.6 64.3 1.0 OE2 B:GLU60 2.6 63.9 1.0 OE2 B:GLU115 2.7 59.5 1.0 O1 B:PL3302 2.7 50.4 1.0 OE1 B:GLU144 2.7 60.2 1.0 CD B:GLU60 2.8 64.3 1.0 OE1 B:GLU115 2.8 54.8 1.0 CD B:GLU144 2.9 60.3 1.0 CE1 B:HIS147 2.9 61.1 1.0 FE B:FE2301 3.0 53.0 1.0 CD B:GLU115 3.1 56.5 1.0 C1 B:PL3302 3.8 52.5 1.0 CG B:HIS147 3.8 59.4 1.0 CG B:GLU60 4.0 70.1 1.0 NE2 B:HIS147 4.2 63.5 1.0 CG B:GLU144 4.3 55.8 1.0 CB B:HIS147 4.5 58.7 1.0 OE1 B:GLU32 4.5 56.3 1.0 CG B:GLU115 4.6 51.4 1.0 CD2 B:HIS147 4.7 60.5 1.0 CE2 B:TYR39 4.7 62.3 1.0 CA B:GLU144 4.7 57.4 1.0 CB B:ALA35 4.8 60.8 1.0 CB B:GLU144 4.8 55.9 1.0 ND1 B:HIS63 4.8 63.7 1.0

Y.Gao, H.Zhang, M.Fan, C.Jia, L.Shi, X.Pan, P.Cao, X.Zhao, W.Chang, M.Li. Structural Insights Into Catalytic Mechanism and Product Delivery of Cyanobacterial Acyl-Acyl Carrier Protein Reductase Nat Commun 2020.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-020-15268-Y