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Zinc in PDB 1ycm: Solution Structure of Matrix Metalloproteinase 12 (MMP12) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh)

Enzymatic activity of Solution Structure of Matrix Metalloproteinase 12 (MMP12) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh)

All present enzymatic activity of Solution Structure of Matrix Metalloproteinase 12 (MMP12) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh):
3.4.24.65;

Other elements in 1ycm:

The structure of Solution Structure of Matrix Metalloproteinase 12 (MMP12) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh) also contains other interesting chemical elements:

Calcium (Ca) 60 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of Matrix Metalloproteinase 12 (MMP12) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh) (pdb code 1ycm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of Matrix Metalloproteinase 12 (MMP12) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh), PDB code: 1ycm:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1ycm

Go back to Zinc Binding Sites List in 1ycm
Zinc binding site 1 out of 2 in the Solution Structure of Matrix Metalloproteinase 12 (MMP12) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of Matrix Metalloproteinase 12 (MMP12) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn264

b:1.0
occ:1.00
NE2 A:HIS218 2.1 0.9 1.0
NE2 A:HIS222 2.1 0.8 1.0
NE2 A:HIS228 2.1 0.9 1.0
HE1 A:HIS218 2.8 3.5 1.0
CE1 A:HIS218 2.9 2.3 1.0
CD2 A:HIS222 3.1 1.0 1.0
CD2 A:HIS228 3.1 1.0 1.0
CE1 A:HIS222 3.2 1.6 1.0
CE1 A:HIS228 3.2 1.1 1.0
CD2 A:HIS218 3.3 1.0 1.0
O4 A:NGH269 3.3 2.8 1.0
HD2 A:HIS222 3.3 1.9 1.0
HD2 A:HIS228 3.3 1.4 1.0
HA A:PRO238 3.4 0.9 1.0
HE1 A:HIS222 3.4 2.3 1.0
HE1 A:HIS228 3.4 1.3 1.0
O5 A:NGH269 3.6 2.0 1.0
HD2 A:HIS218 3.7 2.4 1.0
HE1 A:MET236 3.9 3.5 1.0
ND1 A:HIS218 4.1 2.4 1.0
N1 A:NGH269 4.1 2.5 1.0
HB3 A:PRO238 4.2 1.1 1.0
CG A:HIS228 4.3 1.0 1.0
CG A:HIS222 4.3 0.8 1.0
ND1 A:HIS228 4.3 1.2 1.0
C11 A:NGH269 4.3 2.0 1.0
ND1 A:HIS222 4.3 1.7 1.0
CG A:HIS218 4.3 0.7 1.0
CA A:PRO238 4.4 0.9 1.0
O A:PHE237 4.6 0.9 1.0
O A:MET236 4.8 0.8 1.0
CB A:PRO238 4.9 1.1 1.0
HD1 A:HIS218 4.9 3.6 1.0
CE A:MET236 5.0 3.0 1.0

Zinc binding site 2 out of 2 in 1ycm

Go back to Zinc Binding Sites List in 1ycm
Zinc binding site 2 out of 2 in the Solution Structure of Matrix Metalloproteinase 12 (MMP12) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of Matrix Metalloproteinase 12 (MMP12) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn265

b:1.6
occ:1.00
OD2 A:ASP170 2.1 2.2 1.0
NE2 A:HIS183 2.2 1.3 1.0
NE2 A:HIS168 2.2 2.2 1.0
ND1 A:HIS196 2.5 1.2 1.0
HE1 A:HIS196 3.0 2.5 1.0
CE1 A:HIS168 3.1 3.6 1.0
CE1 A:HIS196 3.1 2.0 1.0
CE1 A:HIS183 3.1 1.0 1.0
CG A:ASP170 3.2 2.0 1.0
HE1 A:HIS168 3.3 4.7 1.0
CD2 A:HIS183 3.3 1.2 1.0
CD2 A:HIS168 3.3 1.5 1.0
HE1 A:HIS183 3.4 1.2 1.0
HB2 A:ASP170 3.4 2.1 1.0
HA A:ALA173 3.5 2.5 1.0
HD2 A:HIS183 3.6 1.5 1.0
HD2 A:HIS168 3.7 1.6 1.0
CB A:ASP170 3.8 1.7 1.0
CG A:HIS196 3.9 1.0 1.0
OD1 A:ASP170 4.1 2.9 1.0
HB3 A:ASP170 4.2 2.1 1.0
O A:ALA173 4.3 2.6 1.0
ND1 A:HIS168 4.3 3.7 1.0
ND1 A:HIS183 4.3 0.8 1.0
HB2 A:HIS196 4.4 1.1 1.0
CG A:HIS183 4.4 0.9 1.0
CG A:HIS168 4.4 2.2 1.0
NE2 A:HIS196 4.4 2.3 1.0
HE2 A:PHE174 4.5 7.4 1.0
CA A:ALA173 4.6 1.9 1.0
CB A:HIS196 4.7 0.7 1.0
HB3 A:HIS196 4.7 1.1 1.0
CD2 A:HIS196 4.8 1.7 1.0
CE2 A:PHE174 4.8 6.1 1.0
O A:HIS172 4.9 3.0 1.0
HD1 A:HIS172 4.9 5.2 1.0
C A:ALA173 4.9 1.8 1.0

Reference:

I.Bertini, V.Calderone, M.Cosenza, M.Fragai, Y.M.Lee, C.Luchinat, S.Mangani, B.Terni, P.Turano. Conformational Variability of Matrix Metalloproteinases: Beyond A Single 3D Structure. Proc.Natl.Acad.Sci.Usa V. 102 5334 2005.
ISSN: ISSN 0027-8424
PubMed: 15809432
DOI: 10.1073/PNAS.0407106102
Page generated: Wed Dec 16 03:14:07 2020

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