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Zinc in PDB 1cge: Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself

Enzymatic activity of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself

All present enzymatic activity of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself:
3.4.24.7;

Protein crystallography data

The structure of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself, PDB code: 1cge was solved by B.Lovejoy, A.M.Hassell, M.A.Luther, D.Weigl, S.R.Jordan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 1.90
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 72.600, 72.600, 75.100, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / n/a

Other elements in 1cge:

The structure of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself (pdb code 1cge). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself, PDB code: 1cge:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1cge

Go back to Zinc Binding Sites List in 1cge
Zinc binding site 1 out of 2 in the Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:16.2
occ:1.00
NE2 A:HIS228 1.9 21.9 1.0
NE2 A:HIS218 2.1 11.5 1.0
NE2 A:HIS222 2.2 16.8 1.0
CD2 A:HIS228 2.8 21.3 1.0
CE1 A:HIS228 3.1 20.7 1.0
CE1 A:HIS218 3.1 14.2 1.0
CD2 A:HIS222 3.1 15.7 1.0
CD2 A:HIS218 3.1 12.0 1.0
CE1 A:HIS222 3.2 16.3 1.0
CG A:HIS228 4.0 20.8 1.0
ND1 A:HIS228 4.1 20.8 1.0
OE1 A:GLU219 4.1 10.7 1.0
ND1 A:HIS218 4.2 13.4 1.0
CG A:HIS218 4.3 11.7 1.0
O A:HOH543 4.3 27.8 1.0
OE2 A:GLU219 4.3 13.8 1.0
CG A:HIS222 4.3 15.3 1.0
ND1 A:HIS222 4.3 15.2 1.0
H1 A:HOH543 4.5 0.0 1.0
CD A:GLU219 4.6 11.0 1.0
CE A:MET236 4.9 11.4 1.0
CA A:PRO238 4.9 17.7 1.0
HD1 A:HIS228 5.0 0.0 1.0

Zinc binding site 2 out of 2 in 1cge

Go back to Zinc Binding Sites List in 1cge
Zinc binding site 2 out of 2 in the Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:22.6
occ:1.00
OD2 A:ASP170 2.0 20.5 1.0
ND1 A:HIS196 2.0 11.1 1.0
NE2 A:HIS183 2.0 22.3 1.0
NE2 A:HIS168 2.0 23.1 1.0
CD2 A:HIS168 2.9 23.3 1.0
CE1 A:HIS183 2.9 21.9 1.0
CG A:ASP170 2.9 22.0 1.0
CE1 A:HIS196 2.9 12.0 1.0
CG A:HIS196 3.0 12.1 1.0
CD2 A:HIS183 3.1 20.8 1.0
CE1 A:HIS168 3.1 23.6 1.0
OD1 A:ASP170 3.2 21.7 1.0
CB A:HIS196 3.5 12.3 1.0
CZ A:PHE185 4.0 24.1 1.0
O A:SER172 4.1 26.7 1.0
ND1 A:HIS183 4.1 21.3 1.0
CG A:HIS168 4.1 23.3 1.0
NE2 A:HIS196 4.1 12.4 1.0
CD2 A:HIS196 4.2 12.6 1.0
ND1 A:HIS168 4.2 22.5 1.0
CG A:HIS183 4.2 20.8 1.0
CB A:ASP170 4.2 24.9 1.0
CE1 A:PHE185 4.3 24.6 1.0
CE2 A:PHE174 4.6 18.1 1.0
H A:SER172 4.7 0.0 1.0
CZ A:PHE174 4.8 17.3 1.0
HD1 A:HIS183 4.9 0.0 1.0
HE2 A:HIS196 4.9 0.0 1.0
CA A:HIS196 5.0 15.8 1.0
C A:SER172 5.0 22.1 1.0
CG2 A:VAL164 5.0 26.4 1.0
H A:ASP170 5.0 0.0 1.0

Reference:

B.Lovejoy, A.M.Hassell, M.A.Luther, D.Weigl, S.R.Jordan. Crystal Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself. Biochemistry V. 33 8207 1994.
ISSN: ISSN 0006-2960
PubMed: 8031754
DOI: 10.1021/BI00193A006
Page generated: Mon Jan 25 16:08:00 2021

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