Zinc in PDB 4aw6: Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1)

All present enzymatic activity of Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1):
3.4.24.84;

The structure of Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1), PDB code: 4aw6 was solved by A.C.W.Pike, Y.Y.Dong, A.Quigley, L.Dong, C.D.O.Cooper, A.Chaikuad, S.Goubin, L.Shrestha, Q.Li, S.Mukhopadhyay, J.Yang, X.Xia, C.A.Shintre, A.J.Barr, G.Berridge, R.Chalk, J.E.Bray, F.Von Delft, A.Bullock, C.Bountra, C.H.Arrowsmith, A.Edwards, N.Burgess-Brown, E.P.Carpenter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.96 / 3.40
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	60.987, 95.451, 131.095, 76.73, 79.64, 72.61
R / Rfree (%)	24.6 / 26.4

The binding sites of Zinc atom in the Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1) (pdb code 4aw6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1), PDB code: 4aw6:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1473 b:0.8 occ:1.00 OE2 A:GLU415 2.1 0.2 1.0 NE2 A:HIS335 2.2 0.1 1.0 NE2 A:HIS339 2.2 0.6 1.0 OE1 A:GLU415 2.5 0.4 1.0 CD A:GLU415 2.6 0.8 1.0 CD2 A:HIS335 3.1 0.8 1.0 CE1 A:HIS335 3.1 0.4 1.0 CD2 A:HIS339 3.2 0.6 1.0 CE1 A:HIS339 3.3 0.7 1.0 OE2 A:GLU336 3.3 0.9 1.0 CG A:GLU415 4.1 0.8 1.0 CG A:HIS335 4.1 0.2 1.0 ND1 A:HIS335 4.2 0.2 1.0 CG A:HIS339 4.4 0.5 1.0 CD A:GLU336 4.4 0.7 1.0 ND1 A:HIS339 4.4 0.9 1.0 NE2 A:HIS459 4.5 0.8 1.0 CB A:ALA418 4.6 0.4 1.0 CA A:GLU415 4.8 0.5 1.0 CB A:GLU415 4.8 0.5 1.0 CD2 A:HIS459 5.0 0.4 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1473 b:0.8 occ:1.00 OE2 B:GLU415 2.0 0.5 1.0 NE2 B:HIS335 2.1 0.6 1.0 NE2 B:HIS339 2.2 0.4 1.0 OE1 B:GLU415 2.5 0.4 1.0 CD B:GLU415 2.6 0.1 1.0 CE1 B:HIS335 3.1 0.4 1.0 CD2 B:HIS335 3.1 0.1 1.0 CE1 B:HIS339 3.2 0.5 1.0 CD2 B:HIS339 3.2 0.9 1.0 OE2 B:GLU336 3.4 0.3 1.0 CG B:GLU415 4.0 1.0 1.0 CG B:HIS335 4.1 0.1 1.0 ND1 B:HIS335 4.1 0.0 1.0 CG B:HIS339 4.4 0.5 1.0 ND1 B:HIS339 4.4 0.1 1.0 CD B:GLU336 4.5 1.0 1.0 NE2 B:HIS459 4.5 0.1 1.0 CB B:ALA418 4.6 0.9 1.0 CA B:GLU415 4.7 0.4 1.0 CB B:GLU415 4.8 0.9 1.0 CD2 B:HIS459 4.9 0.6 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1472 b:85.9 occ:1.00 OE2 D:GLU415 2.1 0.7 1.0 NE2 D:HIS335 2.2 98.8 1.0 NE2 D:HIS339 2.3 0.1 1.0 OE1 D:GLU415 2.6 0.9 1.0 CD D:GLU415 2.6 0.5 1.0 CD2 D:HIS335 3.1 0.1 1.0 CE1 D:HIS335 3.1 0.1 1.0 CD2 D:HIS339 3.2 0.5 1.0 OE2 D:GLU336 3.3 0.5 1.0 CE1 D:HIS339 3.3 0.3 1.0 CG D:GLU415 4.1 0.0 1.0 CG D:HIS335 4.1 0.9 1.0 ND1 D:HIS335 4.2 0.9 1.0 CD D:GLU336 4.4 0.0 1.0 CG D:HIS339 4.4 0.0 1.0 ND1 D:HIS339 4.4 1.0 1.0 NE2 D:HIS459 4.6 0.5 1.0 CB D:ALA418 4.7 99.4 1.0 CA D:GLU415 4.9 97.3 1.0 CB D:GLU415 4.9 96.0 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of the Human Nuclear Membrane Zinc Metalloprotease ZMPSTE24 (FACE1) within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn1472 b:0.9 occ:1.00 OE2 E:GLU415 2.0 0.8 1.0 NE2 E:HIS335 2.2 0.8 1.0 NE2 E:HIS339 2.2 0.4 1.0 CD E:GLU415 2.7 0.7 1.0 OE1 E:GLU415 2.8 0.2 1.0 CD2 E:HIS335 3.0 0.5 1.0 CE1 E:HIS335 3.1 0.4 1.0 CD2 E:HIS339 3.1 0.8 1.0 OE2 E:GLU336 3.2 0.7 1.0 CE1 E:HIS339 3.2 0.8 1.0 CG E:HIS335 4.1 1.0 1.0 CG E:GLU415 4.1 0.8 1.0 ND1 E:HIS335 4.2 1.0 1.0 CD E:GLU336 4.3 0.9 1.0 CG E:HIS339 4.3 0.2 1.0 ND1 E:HIS339 4.4 0.7 1.0 NE2 E:HIS459 4.5 1.0 1.0 CB E:ALA418 4.6 0.4 1.0 CA E:GLU415 4.9 0.6 1.0 CB E:GLU415 4.9 0.1 1.0 OE1 E:GLU336 4.9 0.7 1.0 CD2 E:HIS459 5.0 0.1 1.0

A.Quigley, Y.Y.Dong, A.C.W.Pike, L.Dong, L.Shrestha, G.Berridge, P.J.Stansfeld, M.S.P.Sansom, A.M.Edwards, C.Bountra, F.Von Delft, A.N.Bullock, N.A.Burgess-Brown, E.P.Carpenter. The Structural Basis of ZMPSTE24-Dependent Laminopathies. Science V. 339 1604 2013.
ISSN: ISSN 0036-8075
PubMed: 23539603
DOI: 10.1126/SCIENCE.1231513