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Zinc in PDB 1i76: Complex of 2-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3- Carboxylic Acid (D-Tic Derivative) with T Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form)

Enzymatic activity of Complex of 2-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3- Carboxylic Acid (D-Tic Derivative) with T Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form)

All present enzymatic activity of Complex of 2-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3- Carboxylic Acid (D-Tic Derivative) with T Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form):
3.4.24.34;

Protein crystallography data

The structure of Complex of 2-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3- Carboxylic Acid (D-Tic Derivative) with T Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form), PDB code: 1i76 was solved by E.Gavuzzo, G.Pochetti, F.Mazza, C.Gallina, B.Gorini, S.D'alessio, M.Pieper, H.Tschesche, P.A.Tucker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 32.990, 68.684, 70.584, 90.00, 90.00, 90.00
R / Rfree (%) 12.9 / 17.1

Other elements in 1i76:

The structure of Complex of 2-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3- Carboxylic Acid (D-Tic Derivative) with T Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form) also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Complex of 2-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3- Carboxylic Acid (D-Tic Derivative) with T Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form) (pdb code 1i76). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Complex of 2-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3- Carboxylic Acid (D-Tic Derivative) with T Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form), PDB code: 1i76:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1i76

Go back to Zinc Binding Sites List in 1i76
Zinc binding site 1 out of 2 in the Complex of 2-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3- Carboxylic Acid (D-Tic Derivative) with T Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Complex of 2-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3- Carboxylic Acid (D-Tic Derivative) with T Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn998

b:7.8
occ:1.00
 OD2 A:ASP149 2.0 9.2 1.0
NE2 A:HIS162 2.0 7.3 1.0
NE2 A:HIS147 2.0 6.8 1.0
CD2 A:HIS175 2.0 5.9 1.0
CG A:ASP149 2.9 9.2 1.0
CE1 A:HIS162 2.9 7.5 1.0
CD2 A:HIS147 2.9 7.3 1.0
NE2 A:HIS175 3.0 9.4 1.0
CE1 A:HIS147 3.1 6.9 1.0
CD2 A:HIS162 3.1 7.1 1.0
CG A:HIS175 3.1 7.2 1.0
OD1 A:ASP149 3.2 10.8 1.0
CB A:HIS175 3.5 6.8 1.0
ND1 A:HIS162 4.1 7.3 1.0
CE1 A:HIS175 4.1 7.0 1.0
CG A:HIS147 4.1 6.8 1.0
ND1 A:HIS147 4.1 6.7 1.0
CG A:HIS162 4.2 7.2 1.0
CB A:ASP149 4.2 10.8 1.0
ND1 A:HIS175 4.2 9.4 1.0
O A:SER151 4.3 9.7 1.0
CE1 A:PHE164 4.3 10.8 1.0
CZ A:PHE164 4.5 16.1 1.0
CE2 A:PHE153 4.6 7.0 1.0
CZ A:PHE153 4.6 7.7 1.0
O A:HOH316 4.8 12.4 1.0

Zinc binding site 2 out of 2 in 1i76

Go back to Zinc Binding Sites List in 1i76
Zinc binding site 2 out of 2 in the Complex of 2-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3- Carboxylic Acid (D-Tic Derivative) with T Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Complex of 2-(Biphenyl-4-Sulfonyl)-1,2,3,4-Tetrahydro-Isoquinoline-3- Carboxylic Acid (D-Tic Derivative) with T Catalitic Domain of Matrix Metallo Proteinase-8 (MET80 Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn999

b:7.0
occ:1.00
 NE2 A:HIS197 2.0 6.1 1.0
O45 A:BSI1 2.0 8.8 1.0
NE2 A:HIS201 2.0 6.7 1.0
NE2 A:HIS207 2.0 7.7 1.0
C43 A:BSI1 2.7 8.0 1.0
O46 A:BSI1 2.8 9.1 1.0
CE1 A:HIS201 3.0 9.1 1.0
CE1 A:HIS197 3.0 6.3 1.0
CE1 A:HIS207 3.0 9.5 1.0
CD2 A:HIS197 3.0 6.5 1.0
CD2 A:HIS207 3.0 7.5 1.0
CD2 A:HIS201 3.1 6.8 1.0
ND1 A:HIS197 4.1 6.3 1.0
ND1 A:HIS207 4.1 9.4 1.0
ND1 A:HIS201 4.1 10.3 1.0
CG A:HIS197 4.2 6.0 1.0
C9 A:BSI1 4.2 9.3 1.0
CG A:HIS207 4.2 7.6 1.0
CG A:HIS201 4.2 6.6 1.0
O A:HOH304 4.6 8.6 1.0
CE A:MET215 4.6 7.6 1.0
C3 A:BSI1 4.7 16.6 1.0
OE2 A:GLU198 4.7 7.7 1.0
C4 A:BSI1 4.7 16.2 1.0
C10 A:BSI1 4.7 12.8 1.0
C7 A:BSI1 4.8 13.7 1.0
C16 A:BSI1 4.8 11.5 1.0
N8 A:BSI1 4.8 10.8 1.0
C17 A:BSI1 4.9 11.5 1.0
C21 A:BSI1 4.9 11.9 1.0
O A:HOH386 4.9 24.1 1.0

Reference:

E.Gavuzzo, G.Pochetti, F.Mazza, C.Gallina, B.Gorini, S.D'alessio, M.Pieper, H.Tschesche, P.A.Tucker. Two Crystal Structures of Human Neutrophil Collagenase, One Complexed with A Primed- and the Other with An Unprimed-Side Inhibitor: Implications For Drug Design. J.Med.Chem. V. 43 3377 2000.
ISSN: ISSN 0022-2623
PubMed: 10978185
DOI: 10.1021/JM9909589
Page generated: Sun Oct 13 02:55:35 2024

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