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Zinc in PDB 1hov: Solution Structure of A Catalytic Domain of Mmp-2 Complexed with Sc-74020

Enzymatic activity of Solution Structure of A Catalytic Domain of Mmp-2 Complexed with Sc-74020

All present enzymatic activity of Solution Structure of A Catalytic Domain of Mmp-2 Complexed with Sc-74020:
3.4.24.24;

Other elements in 1hov:

The structure of Solution Structure of A Catalytic Domain of Mmp-2 Complexed with Sc-74020 also contains other interesting chemical elements:

Calcium (Ca) 22 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of A Catalytic Domain of Mmp-2 Complexed with Sc-74020 (pdb code 1hov). 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 A Catalytic Domain of Mmp-2 Complexed with Sc-74020, PDB code: 1hov:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1hov

Go back to Zinc Binding Sites List in 1hov
Zinc binding site 1 out of 2 in the Solution Structure of A Catalytic Domain of Mmp-2 Complexed with Sc-74020


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 A Catalytic Domain of Mmp-2 Complexed with Sc-74020 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn165

b:11.6
occ:1.00
HD1 A:HIS98 1.7 0.0 1.0
NE2 A:HIS85 2.1 0.0 1.0
NE2 A:HIS70 2.1 0.0 1.0
ND1 A:HIS98 2.3 0.0 1.0
OD2 A:ASP72 2.3 0.0 1.0
CE1 A:HIS98 2.8 0.0 1.0
CE1 A:HIS85 2.8 0.0 1.0
HE1 A:HIS98 2.9 0.0 1.0
HE1 A:HIS85 2.9 0.0 1.0
CE1 A:HIS70 3.0 0.0 1.0
HE1 A:HIS70 3.1 0.0 1.0
CG A:ASP72 3.2 0.0 1.0
CD2 A:HIS70 3.3 0.0 1.0
CD2 A:HIS85 3.3 0.0 1.0
CG A:HIS98 3.3 0.0 1.0
HB2 A:HIS98 3.6 0.0 1.0
HD2 A:HIS70 3.6 0.0 1.0
OD1 A:ASP72 3.6 0.0 1.0
HD2 A:HIS85 3.7 0.0 1.0
CB A:HIS98 4.0 0.0 1.0
NE2 A:HIS98 4.0 0.0 1.0
ND1 A:HIS85 4.1 0.0 1.0
ND1 A:HIS70 4.2 0.0 1.0
CD2 A:HIS98 4.2 0.0 1.0
CG A:HIS85 4.3 0.0 1.0
CG A:HIS70 4.3 0.0 1.0
HB3 A:HIS98 4.4 0.0 1.0
HB2 A:ASP72 4.4 0.0 1.0
CB A:ASP72 4.5 0.0 1.0
HA2 A:GLY66 4.8 0.0 1.0
HD1 A:PHE87 4.8 0.0 1.0
HD1 A:HIS85 4.9 0.0 1.0
HB3 A:ASP72 5.0 0.0 1.0

Zinc binding site 2 out of 2 in 1hov

Go back to Zinc Binding Sites List in 1hov
Zinc binding site 2 out of 2 in the Solution Structure of A Catalytic Domain of Mmp-2 Complexed with Sc-74020


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 A Catalytic Domain of Mmp-2 Complexed with Sc-74020 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn166

b:10.6
occ:1.00
NE2 A:HIS130 2.1 0.0 1.0
O1 A:I52800 2.1 20.0 1.0
O26 A:I52800 2.1 20.0 1.0
NE2 A:HIS120 2.2 0.0 1.0
NE2 A:HIS124 2.3 0.0 1.0
C3 A:I52800 2.7 20.0 1.0
N2 A:I52800 2.7 20.0 1.0
CE1 A:HIS130 2.8 0.0 1.0
HE1 A:HIS130 2.8 0.0 1.0
H1 A:I52800 2.9 20.0 1.0
CD2 A:HIS124 2.9 0.0 1.0
HD2 A:HIS124 3.0 0.0 1.0
CE1 A:HIS120 3.2 0.0 1.0
CD2 A:HIS120 3.2 0.0 1.0
CE1 A:HIS124 3.2 0.0 1.0
CD2 A:HIS130 3.3 0.0 1.0
HE1 A:HIS120 3.4 0.0 1.0
HD2 A:HIS120 3.4 0.0 1.0
H2 A:I52800 3.7 20.0 1.0
HE1 A:HIS124 3.7 0.0 1.0
HD2 A:HIS130 3.7 0.0 1.0
CG A:HIS124 4.0 0.0 1.0
ND1 A:HIS130 4.1 0.0 1.0
ND1 A:HIS124 4.1 0.0 1.0
C4 A:I52800 4.1 20.0 1.0
CG A:HIS130 4.3 0.0 1.0
ND1 A:HIS120 4.3 0.0 1.0
H62 A:I52800 4.4 20.0 1.0
CG A:HIS120 4.4 0.0 1.0
C16 A:I52800 4.5 20.0 1.0
N5 A:I52800 4.5 20.0 1.0
H61 A:I52800 4.6 20.0 1.0
H16 A:I52800 4.6 20.0 2.0
H4 A:I52800 4.6 20.0 1.0
C17 A:I52800 4.6 20.0 1.0
C6 A:I52800 4.8 20.0 1.0
HA A:MET138 4.8 0.0 1.0
OE2 A:GLU121 4.8 0.0 1.0
H17 A:I52800 4.8 20.0 2.0
C15 A:I52800 4.8 20.0 1.0
H23 A:I52800 4.8 20.0 1.0
HD1 A:HIS130 4.9 0.0 1.0
O A:MET138 4.9 0.0 1.0
HD1 A:HIS124 5.0 0.0 1.0

Reference:

Y.Feng, J.J.Likos, L.Zhu, H.Woodward, G.Munie, J.J.Mcdonald, A.M.Stevens, C.P.Howard, G.A.De Crescenzo, D.Welsch, H.-S.Shieh, W.C.Stallings. Solution Structure and Backbone Dynamics of the Catalytic Domain of Matrix Metalloproteinase-2 Complexed with A Hydroxamic Acid Inhibitor Biochim.Biophys.Acta V.1598 10 2002.
ISSN: ISSN 0006-3002
PubMed: 12147339
DOI: 10.1016/S0167-4838(02)00307-2
Page generated: Wed Dec 16 02:51:28 2020

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