Atomistry » Zinc » PDB 1hxy-1i95 » 1i76
Atomistry »
  Zinc »
    PDB 1hxy-1i95 »
      1i76 »

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: Wed Dec 16 02:52:24 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy