Atomistry » Zinc » PDB 2mls-2n95 » 2n8r
Atomistry »
  Zinc »
    PDB 2mls-2n95 »
      2n8r »

Zinc in PDB 2n8r: Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr)

Enzymatic activity of Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr)

All present enzymatic activity of Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr):
3.4.24.65;

Other elements in 2n8r:

The structure of Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr) also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr) (pdb code 2n8r). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr), PDB code: 2n8r:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2n8r

Go back to Zinc Binding Sites List in 2n8r
Zinc binding site 1 out of 2 in the Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:0.0
occ:1.00
O A:HOH401 1.9 0.0 1.0
O D:GLY88 1.9 0.0 1.0
O D:PRO87 2.1 0.0 1.0
NE2 A:HIS218 2.1 0.0 1.0
NE2 A:HIS222 2.1 0.0 1.0
NE2 A:HIS228 2.1 0.0 1.0
H1 A:HOH401 2.7 0.0 1.0
H2 A:HOH401 2.7 0.0 1.0
C D:GLY88 3.0 0.0 1.0
CE1 A:HIS228 3.0 0.0 1.0
CD2 A:HIS222 3.1 0.0 1.0
CE1 A:HIS218 3.1 0.0 1.0
C D:PRO87 3.1 0.0 1.0
CD2 A:HIS218 3.2 0.0 1.0
CE1 A:HIS222 3.2 0.0 1.0
HE1 A:HIS228 3.2 0.0 1.0
CD2 A:HIS228 3.2 0.0 1.0
HD2 A:HIS222 3.3 0.0 1.0
HE1 A:HIS218 3.4 0.0 1.0
HD2 A:HIS218 3.4 0.0 1.0
HE1 A:HIS222 3.5 0.0 1.0
HA2 D:GLY88 3.5 0.0 1.0
CA D:GLY88 3.6 0.0 1.0
HD2 A:HIS228 3.6 0.0 1.0
HB D:VAL89 3.6 0.0 1.0
N D:GLY88 3.7 0.0 1.0
HG12 D:VAL89 3.9 0.0 1.0
OE2 A:GLU219 4.0 0.0 1.0
N D:VAL89 4.1 0.0 1.0
HE3 A:MET236 4.1 0.0 1.0
ND1 A:HIS228 4.2 0.0 1.0
ND1 A:HIS218 4.2 0.0 1.0
CG A:HIS222 4.2 0.0 1.0
CG A:HIS218 4.3 0.0 1.0
CG A:HIS228 4.3 0.0 1.0
ND1 A:HIS222 4.3 0.0 1.0
CB D:VAL89 4.4 0.0 1.0
HE1 A:MET236 4.4 0.0 1.0
CA D:PRO87 4.4 0.0 1.0
CG1 D:VAL89 4.5 0.0 1.0
HB2 C:PRO51 4.5 0.0 1.0
O C:GLY52 4.6 0.0 1.0
HA3 D:GLY88 4.6 0.0 1.0
H D:GLY88 4.7 0.0 1.0
CA D:VAL89 4.7 0.0 1.0
HG11 D:VAL89 4.7 0.0 1.0
H C:GLY52 4.7 0.0 1.0
CE A:MET236 4.8 0.0 1.0
N D:PRO87 4.8 0.0 1.0
HA A:PRO238 4.8 0.0 1.0
HB2 D:PRO87 4.8 0.0 1.0
HA D:VAL89 4.9 0.0 1.0
H D:VAL89 4.9 0.0 1.0
O D:PRO86 4.9 0.0 1.0
CD A:GLU219 4.9 0.0 1.0

Zinc binding site 2 out of 2 in 2n8r

Go back to Zinc Binding Sites List in 2n8r
Zinc binding site 2 out of 2 in the Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Productive Complex Between Mmp-12 and Synthetic Triple-Helical Collagen, Revealed Through Paramagnetic uc(Nmr) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:0.0
occ:1.00
OD1 A:ASP170 1.8 0.0 1.0
NE2 A:HIS168 2.1 0.0 1.0
NE2 A:HIS183 2.1 0.0 1.0
ND1 A:HIS196 2.1 0.0 1.0
OD2 A:ASP170 2.1 0.0 1.0
CG A:ASP170 2.4 0.0 1.0
CE1 A:HIS196 2.9 0.0 1.0
CD2 A:HIS168 2.9 0.0 1.0
CE1 A:HIS183 3.0 0.0 1.0
HE1 A:HIS196 3.0 0.0 1.0
CE1 A:HIS168 3.1 0.0 1.0
HE1 A:HIS183 3.1 0.0 1.0
HD2 A:HIS168 3.2 0.0 1.0
CD2 A:HIS183 3.3 0.0 1.0
CG A:HIS196 3.3 0.0 1.0
HE1 A:HIS168 3.5 0.0 1.0
HD2 A:HIS183 3.6 0.0 1.0
HB2 A:HIS172 3.7 0.0 1.0
HB2 A:HIS196 3.7 0.0 1.0
CB A:ASP170 3.8 0.0 1.0
HB3 A:HIS196 3.9 0.0 1.0
CG A:HIS168 3.9 0.0 1.0
CB A:HIS196 3.9 0.0 1.0
ND1 A:HIS168 4.0 0.0 1.0
NE2 A:HIS196 4.1 0.0 1.0
ND1 A:HIS183 4.2 0.0 1.0
HB3 A:ASP170 4.2 0.0 1.0
H A:ASP170 4.2 0.0 1.0
O A:HIS168 4.3 0.0 1.0
CD2 A:HIS196 4.3 0.0 1.0
HE2 A:PHE185 4.3 0.0 1.0
CG A:HIS183 4.3 0.0 1.0
N A:ASP170 4.4 0.0 1.0
HB2 A:ASP170 4.5 0.0 1.0
HD2 A:HIS172 4.5 0.0 1.0
CA A:ASP170 4.6 0.0 1.0
CB A:HIS172 4.7 0.0 1.0
CE2 A:PHE185 4.8 0.0 1.0
C A:HIS168 4.9 0.0 1.0
HD1 A:HIS168 4.9 0.0 1.0
H A:HIS172 5.0 0.0 1.0
HE2 A:HIS196 5.0 0.0 1.0

Reference:

S.H.Prior, T.S.Byrne, D.Tokmina-Roszyk, G.B.Fields, S.R.Van Doren. Path to Collagenolysis: Collagen V Triple-Helix Model Bound Productively and in Encounters By Matrix Metalloproteinase-12. J.Biol.Chem. V. 291 7888 2016.
ISSN: ISSN 0021-9258
PubMed: 26887942
DOI: 10.1074/JBC.M115.703124
Page generated: Wed Dec 16 03:41:56 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy