Zinc in PDB 8vjw: Structure of Human Neurolysin in Complex with Angiotensin I Peptide

All present enzymatic activity of Structure of Human Neurolysin in Complex with Angiotensin I Peptide:
3.4.24.16;

The structure of Structure of Human Neurolysin in Complex with Angiotensin I Peptide, PDB code: 8vjw was solved by K.Shi, H.Aihara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.99 / 2.49
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	101.078, 60.584, 147.759, 90, 106.57, 90
R / Rfree (%)	23.7 / 28.7

The binding sites of Zinc atom in the Structure of Human Neurolysin in Complex with Angiotensin I Peptide (pdb code 8vjw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Human Neurolysin in Complex with Angiotensin I Peptide, PDB code: 8vjw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Human Neurolysin in Complex with Angiotensin I Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Neurolysin in Complex with Angiotensin I Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:136.5 occ:1.00 O C:TYR4 1.9 78.0 0.9 NE2 A:HIS474 2.0 62.8 1.0 NE2 A:HIS478 2.0 71.8 1.0 CE1 A:HIS474 2.6 59.7 1.0 CD2 A:HIS478 2.7 63.5 1.0 C C:TYR4 2.9 76.1 0.9 CD2 A:HIS474 3.1 53.0 1.0 OE2 A:GLU503 3.1 59.5 1.0 OE1 A:GLU503 3.2 50.4 1.0 CE1 A:HIS478 3.2 55.6 1.0 CD A:GLU503 3.5 51.1 1.0 OG A:SER506 3.7 45.7 1.0 ND1 A:HIS474 3.8 43.3 1.0 N D:ILE5 3.8 68.2 1.0 CG A:HIS478 3.9 52.8 1.0 OE2 A:GLU475 4.0 61.6 1.0 CB A:SER506 4.0 36.5 1.0 CG A:HIS474 4.0 43.3 1.0 ND1 A:HIS478 4.2 45.8 1.0 CA D:ILE5 4.2 71.6 1.0 CA C:TYR4 4.2 75.7 0.9 OE1 A:GLU475 4.4 50.2 1.0 O C:VAL3 4.5 77.3 0.9 CD A:GLU475 4.5 55.0 1.0 N C:TYR4 4.7 76.2 0.9 C C:VAL3 4.7 77.0 0.9 CB D:ILE5 4.9 68.4 1.0

Zinc binding site 2 out of 2 in the Structure of Human Neurolysin in Complex with Angiotensin I Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Human Neurolysin in Complex with Angiotensin I Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:149.4 occ:1.00 O E:TYR4 2.0 84.8 0.9 OE2 B:GLU503 2.1 81.3 1.0 OE1 B:GLU503 2.1 70.0 1.0 NE2 B:HIS478 2.1 83.4 1.0 NE2 B:HIS474 2.1 59.5 1.0 CD B:GLU503 2.4 67.7 1.0 CE1 B:HIS474 2.9 62.1 1.0 C E:TYR4 2.9 81.2 0.9 CD2 B:HIS478 3.0 57.6 1.0 CE1 B:HIS478 3.1 65.7 1.0 CD2 B:HIS474 3.3 49.2 1.0 OG B:SER506 3.4 47.1 1.0 CG B:GLU503 3.9 46.0 1.0 CB B:SER506 3.9 37.9 1.0 ND1 B:HIS474 4.1 52.9 1.0 CG B:HIS478 4.1 47.3 1.0 ND1 B:HIS478 4.2 48.5 1.0 N F:ILE5 4.2 45.9 0.9 CG B:HIS474 4.3 43.0 1.0 CA E:TYR4 4.4 81.6 0.9 CA F:ILE5 4.4 53.1 0.9 OE2 B:GLU475 4.6 49.4 1.0 CE1 B:TYR613 4.6 44.4 1.0 CB B:GLU503 4.7 40.8 1.0 CA B:GLU503 4.8 46.8 1.0 OH B:TYR613 4.9 49.9 1.0 N E:TYR4 4.9 81.9 0.9 CB E:TYR4 5.0 82.5 0.9

H.Aihara, K.Shi, H.Aihara. N/A N/A.