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Zinc in PDB 1cgl: Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor

Enzymatic activity of Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor

All present enzymatic activity of Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor:
3.4.24.7;

Protein crystallography data

The structure of Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor, PDB code: 1cgl was solved by B.Lovejoy, A.Cleasby, A.M.Hassell, K.Longley, M.A.Luther, D.Weigl, G.Mcgeehan, A.B.Mcelroy, D.Drewry, M.H.Lambert, S.R.Jordan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 2.40
Space group P 64
Cell size a, b, c (Å), α, β, γ (°) 78.200, 78.200, 87.400, 90.00, 90.00, 120.00
R / Rfree (%) 18.6 / n/a

Other elements in 1cgl:

The structure of Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor (pdb code 1cgl). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor, PDB code: 1cgl:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1cgl

Go back to Zinc Binding Sites List in 1cgl
Zinc binding site 1 out of 4 in the Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:22.2
occ:1.00
 NE2 A:HIS228 2.0 20.5 1.0
OE2 A:0ED1 2.0 25.2 1.0
NE2 A:HIS222 2.1 14.4 1.0
NE2 A:HIS218 2.2 19.1 1.0
OE1 A:0ED1 2.6 27.7 1.0
CD A:0ED1 2.7 24.7 1.0
CD2 A:HIS228 2.9 21.1 1.0
CD2 A:HIS218 3.1 21.2 1.0
CE1 A:HIS222 3.1 14.2 1.0
CE1 A:HIS228 3.1 21.2 1.0
CD2 A:HIS222 3.1 14.9 1.0
CE1 A:HIS218 3.2 20.4 1.0
HD11 A:0ED1 3.6 0.0 1.0
HB21 A:0ED1 4.0 0.0 1.0
HA A:0ED1 4.0 0.0 1.0
CG A:HIS228 4.1 22.9 1.0
ND1 A:HIS228 4.2 23.5 1.0
CG A:0ED1 4.2 21.6 1.0
ND1 A:HIS222 4.2 13.8 1.0
CG A:HIS222 4.3 13.4 1.0
CG A:HIS218 4.3 19.5 1.0
ND1 A:HIS218 4.3 19.7 1.0
H2 A:HOH922 4.4 0.0 1.0
CE A:MET236 4.5 14.2 1.0
O A:HOH922 4.5 15.6 1.0
CA1 A:0ED1 4.7 17.1 1.0
N1 A:0ED1 4.7 21.4 1.0
CD1 A:0ED1 4.7 14.9 1.0
HG1 A:0ED1 4.7 0.0 1.0
CB1 A:0ED1 4.8 18.0 1.0
OE1 A:GLU219 4.8 16.4 1.0
H1 A:HOH922 4.8 0.0 1.0
OE2 A:GLU219 4.8 19.8 1.0
HB1 A:0ED1 4.9 0.0 1.0
O A:TYR237 5.0 11.7 1.0

Zinc binding site 2 out of 4 in 1cgl

Go back to Zinc Binding Sites List in 1cgl
Zinc binding site 2 out of 4 in the Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:28.1
occ:1.00
 ND1 A:HIS196 2.0 34.0 1.0
NE2 A:HIS168 2.0 25.8 1.0
NE2 A:HIS183 2.2 20.1 1.0
OD2 A:ASP170 2.2 45.1 1.0
CG A:ASP170 2.8 43.1 1.0
CE1 A:HIS196 2.8 32.1 1.0
OD1 A:ASP170 2.8 44.2 1.0
CD2 A:HIS168 2.8 26.6 1.0
CE1 A:HIS183 3.1 21.1 1.0
CG A:HIS196 3.2 33.5 1.0
CE1 A:HIS168 3.2 28.4 1.0
CD2 A:HIS183 3.3 20.6 1.0
CB A:HIS196 3.7 30.0 1.0
NE2 A:HIS196 4.0 34.1 1.0
O A:SER172 4.1 30.5 1.0
CG A:HIS168 4.1 26.1 1.0
CB A:ASP170 4.1 42.7 1.0
CZ A:PHE185 4.1 27.8 1.0
CD2 A:HIS196 4.2 32.1 1.0
ND1 A:HIS168 4.2 27.2 1.0
ND1 A:HIS183 4.3 17.4 1.0
CG A:HIS183 4.4 19.0 1.0
CE2 A:PHE185 4.5 29.7 1.0
H71 A:0ED1 4.7 0.0 1.0
CE2 A:PHE174 4.7 13.8 1.0
CZ A:PHE174 4.7 10.6 1.0
HE2 A:HIS196 4.9 0.0 1.0
H A:SER172 5.0 0.0 1.0

Zinc binding site 3 out of 4 in 1cgl

Go back to Zinc Binding Sites List in 1cgl
Zinc binding site 3 out of 4 in the Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:19.3
occ:1.00
 NE2 B:HIS228 2.0 16.7 1.0
NE2 B:HIS222 2.0 17.9 1.0
OE2 B:0ED1 2.1 23.1 1.0
NE2 B:HIS218 2.2 11.8 1.0
OE1 B:0ED1 2.7 20.1 1.0
CD2 B:HIS222 2.8 15.7 1.0
CD B:0ED1 2.8 20.4 1.0
CE1 B:HIS228 2.9 17.0 1.0
CD2 B:HIS218 3.0 15.1 1.0
CD2 B:HIS228 3.1 19.1 1.0
CE1 B:HIS222 3.2 15.2 1.0
CE1 B:HIS218 3.3 12.7 1.0
HD11 B:0ED1 3.8 0.0 1.0
ND1 B:HIS228 4.0 18.7 1.0
CG B:HIS222 4.0 17.3 1.0
HB21 B:0ED1 4.1 0.0 1.0
CG B:HIS228 4.1 20.1 1.0
HA B:0ED1 4.2 0.0 1.0
ND1 B:HIS222 4.2 18.3 1.0
H2 B:HOH921 4.2 0.0 1.0
CG B:HIS218 4.2 13.2 1.0
CG B:0ED1 4.3 17.9 1.0
O B:HOH920 4.3 32.3 1.0
ND1 B:HIS218 4.4 11.7 1.0
O B:HOH921 4.4 19.9 1.0
OE2 B:GLU219 4.4 13.9 1.0
CE B:MET236 4.6 13.3 1.0
OE1 B:GLU219 4.6 12.9 1.0
H2 B:HOH920 4.7 0.0 1.0
H1 B:HOH921 4.8 0.0 1.0
HG1 B:0ED1 4.8 0.0 1.0
N1 B:0ED1 4.8 14.7 1.0
CA1 B:0ED1 4.8 14.7 1.0
CD1 B:0ED1 4.8 10.4 1.0
HD1 B:HIS228 4.9 0.0 1.0
CD B:GLU219 4.9 13.6 1.0
CB1 B:0ED1 4.9 13.6 1.0

Zinc binding site 4 out of 4 in 1cgl

Go back to Zinc Binding Sites List in 1cgl
Zinc binding site 4 out of 4 in the Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn302

b:22.3
occ:1.00
 OD2 B:ASP170 2.1 24.0 1.0
NE2 B:HIS183 2.1 14.8 1.0
NE2 B:HIS168 2.2 26.7 1.0
ND1 B:HIS196 2.2 24.2 1.0
CG B:ASP170 2.8 22.8 1.0
CE1 B:HIS196 3.0 24.4 1.0
CE1 B:HIS183 3.0 19.0 1.0
CD2 B:HIS168 3.0 26.0 1.0
CE1 B:HIS168 3.2 26.9 1.0
CD2 B:HIS183 3.2 20.1 1.0
OD1 B:ASP170 3.3 23.9 1.0
CG B:HIS196 3.4 25.3 1.0
CB B:HIS196 3.8 24.6 1.0
O B:SER172 3.9 31.8 1.0
CB B:ASP170 4.0 24.3 1.0
ND1 B:HIS183 4.2 20.8 1.0
CG B:HIS168 4.2 24.9 1.0
NE2 B:HIS196 4.2 25.0 1.0
ND1 B:HIS168 4.3 25.8 1.0
CG B:HIS183 4.3 21.2 1.0
H71 B:0ED1 4.3 0.0 1.0
CD2 B:HIS196 4.4 24.9 1.0
CE2 B:PHE185 4.6 18.7 1.0
CZ B:PHE185 4.7 18.0 1.0
CE2 B:PHE174 4.7 15.8 1.0
H B:SER172 4.8 0.0 1.0
CZ B:PHE174 4.8 13.3 1.0
C B:SER172 4.9 25.1 1.0
CB B:SER172 5.0 28.3 1.0

Reference:

B.Lovejoy, A.Cleasby, A.M.Hassell, K.Longley, M.A.Luther, D.Weigl, G.Mcgeehan, A.B.Mcelroy, D.Drewry, M.H.Lambert, S.R.Jordan. Structure of the Catalytic Domain of Fibroblast Collagenase Complexed with An Inhibitor. Science V. 263 375 1994.
ISSN: ISSN 0036-8075
PubMed: 8278810
Page generated: Sat Oct 12 23:06:03 2024

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