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Zinc in PDB 2jnp: Solution Structure of Matrix Metalloproteinase 3 (Mmp-3) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh)

Enzymatic activity of Solution Structure of Matrix Metalloproteinase 3 (Mmp-3) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh)

All present enzymatic activity of Solution Structure of Matrix Metalloproteinase 3 (Mmp-3) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh):
3.4.24.17;

Other elements in 2jnp:

The structure of Solution Structure of Matrix Metalloproteinase 3 (Mmp-3) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh) also contains other interesting chemical elements:

Calcium (Ca) 50 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of Matrix Metalloproteinase 3 (Mmp-3) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh) (pdb code 2jnp). 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 3 (Mmp-3) in the Presence of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]Glycyl Hydroxamic Acid (Nngh), PDB code: 2jnp:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2jnp

Go back to Zinc Binding Sites List in 2jnp
Zinc binding site 1 out of 2 in the Solution Structure of Matrix Metalloproteinase 3 (Mmp-3) 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 3 (Mmp-3) 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:Zn249

b:0.0
occ:1.00
NE2 A:HIS151 2.3 0.0 1.0
NE2 A:HIS166 2.5 0.0 1.0
OD2 A:ASP153 2.5 0.0 1.0
ND1 A:HIS179 2.8 0.0 1.0
CE1 A:HIS166 2.9 0.0 1.0
HE1 A:HIS166 3.0 0.0 1.0
HE1 A:HIS179 3.2 0.0 1.0
CD2 A:HIS151 3.3 0.0 1.0
CE1 A:HIS151 3.3 0.0 1.0
CG A:ASP153 3.3 0.0 1.0
CE1 A:HIS179 3.4 0.0 1.0
HD2 A:HIS151 3.4 0.0 1.0
HE1 A:HIS151 3.5 0.0 1.0
OD1 A:ASP153 3.5 0.0 1.0
CD2 A:HIS166 3.5 0.0 1.0
HE2 A:TYR168 3.6 0.0 1.0
HH A:TYR168 3.7 0.0 1.0
ND1 A:HIS166 4.0 0.0 1.0
HD2 A:HIS166 4.1 0.0 1.0
CG A:HIS179 4.1 0.0 1.0
HB2 A:HIS179 4.3 0.0 1.0
OH A:TYR168 4.3 0.0 1.0
CG A:HIS166 4.3 0.0 1.0
CE2 A:TYR168 4.3 0.0 1.0
CG A:HIS151 4.4 0.0 1.0
ND1 A:HIS151 4.4 0.0 1.0
NE2 A:HIS179 4.6 0.0 1.0
CZ A:TYR168 4.7 0.0 1.0
CB A:ASP153 4.8 0.0 1.0
CB A:HIS179 4.8 0.0 1.0
HD1 A:PHE154 4.8 0.0 1.0
HD1 A:HIS166 4.8 0.0 1.0

Zinc binding site 2 out of 2 in 2jnp

Go back to Zinc Binding Sites List in 2jnp
Zinc binding site 2 out of 2 in the Solution Structure of Matrix Metalloproteinase 3 (Mmp-3) 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 3 (Mmp-3) 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:Zn250

b:0.0
occ:1.00
NE2 A:HIS211 2.3 0.0 1.0
O4 A:NGH253 2.4 0.0 1.0
O5 A:NGH253 2.4 0.0 1.0
NE2 A:HIS201 2.5 0.0 1.0
CD2 A:HIS205 2.7 0.0 1.0
N1 A:NGH253 2.8 0.0 1.0
NE2 A:HIS205 2.8 0.0 1.0
C11 A:NGH253 2.8 0.0 1.0
HD2 A:HIS205 2.9 0.0 1.0
CG A:HIS205 3.2 0.0 1.0
CE1 A:HIS211 3.3 0.0 1.0
CD2 A:HIS211 3.3 0.0 1.0
CE1 A:HIS205 3.4 0.0 1.0
CD2 A:HIS201 3.5 0.0 1.0
HE1 A:HIS211 3.5 0.0 1.0
CE1 A:HIS201 3.5 0.0 1.0
HD2 A:HIS211 3.5 0.0 1.0
ND1 A:HIS205 3.6 0.0 1.0
HN1 A:NGH253 3.6 0.0 1.0
HD2 A:HIS201 3.6 0.0 1.0
HE1 A:HIS201 3.7 0.0 1.0
HB2 A:HIS205 3.9 0.0 1.0
HE1 A:HIS205 4.1 0.0 1.0
CB A:HIS205 4.1 0.0 1.0
H92 A:NGH253 4.1 0.0 1.0
C10 A:NGH253 4.2 0.0 1.0
HE3 A:MET219 4.4 0.0 1.0
HD1 A:HIS205 4.4 0.0 1.0
ND1 A:HIS211 4.5 0.0 1.0
CG A:HIS211 4.5 0.0 1.0
N A:NGH253 4.5 0.0 1.0
HB3 A:HIS205 4.5 0.0 1.0
HE2 A:MET219 4.6 0.0 1.0
ND1 A:HIS201 4.7 0.0 1.0
CG A:HIS201 4.7 0.0 1.0
H102 A:NGH253 4.7 0.0 1.0
C9 A:NGH253 4.7 0.0 1.0
H91 A:NGH253 4.7 0.0 1.0
HA A:HIS166 4.8 0.0 1.0
H101 A:NGH253 4.8 0.0 1.0
H A:ALA167 4.9 0.0 1.0
CE A:MET219 5.0 0.0 1.0

Reference:

L.A.Alcaraz, L.Banci, I.Bertini, F.Cantini, A.Donaire, L.Gonnelli. Matrix Metalloproteinase-Inhibitor Interaction: the Solution Structure of the Catalytic Domain of Human Matrix Metalloproteinase-3 with Different Inhibitors J.Biol.Inorg.Chem. V. 12 1197 2007.
ISSN: ISSN 0949-8257
PubMed: 17710450
DOI: 10.1007/S00775-007-0288-9
Page generated: Thu Oct 17 01:18:45 2024

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