Zinc in PDB 1i1i: Neurolysin (Endopeptidase 24.16) Crystal Structure

All present enzymatic activity of Neurolysin (Endopeptidase 24.16) Crystal Structure:
3.4.24.16;

The structure of Neurolysin (Endopeptidase 24.16) Crystal Structure, PDB code: 1i1i was solved by C.K.Brown, K.Madauss, W.Lian, W.D.Tolbert, M.R.Beck, D.W.Rodgers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	157.600, 87.700, 58.300, 90.00, 90.00, 90.00
R / Rfree (%)	22.4 / 26.8

The binding sites of Zinc atom in the Neurolysin (Endopeptidase 24.16) Crystal Structure (pdb code 1i1i). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Neurolysin (Endopeptidase 24.16) Crystal Structure, PDB code: 1i1i:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Neurolysin (Endopeptidase 24.16) Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Neurolysin (Endopeptidase 24.16) Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn701 b:24.8 occ:1.00 OE1 P:GLU503 2.0 22.4 1.0 NE2 P:HIS474 2.2 22.1 1.0 NE2 P:HIS478 2.2 19.4 1.0 O P:HOH703 2.6 14.2 1.0 CD P:GLU503 2.7 19.5 1.0 OE2 P:GLU503 2.8 20.1 1.0 CD2 P:HIS478 3.1 18.3 1.0 CD2 P:HIS474 3.1 21.3 1.0 CE1 P:HIS474 3.1 22.8 1.0 CE1 P:HIS478 3.2 18.6 1.0 OG P:SER506 3.6 25.5 1.0 CB P:SER506 4.1 22.4 1.0 CG P:GLU503 4.2 17.1 1.0 O P:HOH832 4.2 24.2 1.0 ND1 P:HIS474 4.2 21.1 1.0 CG P:HIS474 4.3 21.4 1.0 ND1 P:HIS478 4.3 19.1 1.0 OE2 P:GLU475 4.3 32.3 1.0 CG P:HIS478 4.3 20.0 1.0 CB P:GLU503 4.9 15.4 1.0

Zinc binding site 2 out of 2 in the Neurolysin (Endopeptidase 24.16) Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Neurolysin (Endopeptidase 24.16) Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn702 b:47.4 occ:1.00 OE2 P:GLU164 1.8 52.1 1.0 NE2 P:HIS160 2.1 29.2 1.0 O P:HOH817 2.3 34.3 1.0 CD P:GLU164 2.7 50.9 1.0 CE1 P:HIS160 3.0 31.5 1.0 CD2 P:HIS160 3.2 32.5 1.0 OE1 P:GLU164 3.2 51.7 1.0 CG P:GLU164 3.8 48.6 1.0 ND1 P:HIS160 4.1 31.1 1.0 CG P:HIS160 4.2 31.7 1.0 CB P:GLU164 5.0 44.2 1.0

C.K.Brown, K.Madauss, W.Lian, M.R.Beck, W.D.Tolbert, D.W.Rodgers. Structure of Neurolysin Reveals A Deep Channel That Limits Substrate Access. Proc.Natl.Acad.Sci.Usa V. 98 3127 2001.
ISSN: ISSN 0027-8424
PubMed: 11248043
DOI: 10.1073/PNAS.051633198