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Zinc in PDB 1mmp: Matrilysin Complexed with Carboxylate Inhibitor

Enzymatic activity of Matrilysin Complexed with Carboxylate Inhibitor

All present enzymatic activity of Matrilysin Complexed with Carboxylate Inhibitor:
3.4.24.23;

Protein crystallography data

The structure of Matrilysin Complexed with Carboxylate Inhibitor, PDB code: 1mmp was solved by M.F.Browner, W.W.Smith, A.L.Castelhano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.30
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 62.000, 62.000, 175.700, 90.00, 90.00, 120.00
R / Rfree (%) 18 / n/a

Other elements in 1mmp:

The structure of Matrilysin Complexed with Carboxylate Inhibitor also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Matrilysin Complexed with Carboxylate Inhibitor (pdb code 1mmp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Matrilysin Complexed with Carboxylate Inhibitor, PDB code: 1mmp:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1mmp

Go back to Zinc Binding Sites List in 1mmp
Zinc binding site 1 out of 4 in the Matrilysin Complexed with Carboxylate Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Matrilysin Complexed with Carboxylate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:14.2
occ:1.00
O2 A:RSS269 2.0 10.3 1.0
NE2 A:HIS228 2.1 13.5 1.0
NE2 A:HIS218 2.1 10.3 1.0
NE2 A:HIS222 2.2 10.4 1.0
O1 A:RSS269 2.7 11.3 1.0
C1 A:RSS269 2.8 10.7 1.0
CE1 A:HIS228 3.0 14.2 1.0
CD2 A:HIS218 3.1 10.9 1.0
CD2 A:HIS222 3.1 11.4 1.0
CE1 A:HIS218 3.1 12.1 1.0
CE1 A:HIS222 3.1 12.4 1.0
CD2 A:HIS228 3.1 12.3 1.0
O A:HOH318 4.0 20.9 1.0
ND1 A:HIS228 4.1 12.6 1.0
C2 A:RSS269 4.2 10.1 1.0
CG A:HIS228 4.2 13.0 1.0
ND1 A:HIS218 4.2 10.1 1.0
ND1 A:HIS222 4.2 11.3 1.0
CG A:HIS218 4.2 10.5 1.0
CG A:HIS222 4.2 10.5 1.0
C3 A:RSS269 4.5 10.7 1.0
CE A:MET236 4.6 5.7 1.0
OE2 A:GLU219 4.7 11.6 1.0
OE1 A:GLU219 4.9 13.4 1.0
C13 A:RSS269 4.9 11.4 1.0

Zinc binding site 2 out of 4 in 1mmp

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Zinc binding site 2 out of 4 in the Matrilysin Complexed with Carboxylate Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Matrilysin Complexed with Carboxylate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2

b:12.0
occ:1.00
NE2 A:HIS168 2.0 11.4 1.0
OD2 A:ASP170 2.0 28.6 1.0
NE2 A:HIS183 2.0 11.6 1.0
ND1 A:HIS196 2.1 10.7 1.0
CG A:ASP170 2.7 27.1 1.0
OD1 A:ASP170 2.7 26.8 1.0
CD2 A:HIS168 2.9 12.8 1.0
CE1 A:HIS183 2.9 12.6 1.0
CE1 A:HIS168 3.0 11.1 1.0
CE1 A:HIS196 3.0 12.1 1.0
CD2 A:HIS183 3.0 11.6 1.0
CG A:HIS196 3.2 10.2 1.0
CB A:HIS196 3.6 7.1 1.0
CB A:ASP170 4.0 25.8 1.0
O A:TYR172 4.0 21.0 1.0
ND1 A:HIS183 4.1 12.1 1.0
CG A:HIS168 4.1 14.6 1.0
ND1 A:HIS168 4.1 12.1 1.0
CG A:HIS183 4.1 12.8 1.0
NE2 A:HIS196 4.2 13.2 1.0
CD2 A:HIS196 4.4 12.3 1.0
CZ A:PHE185 4.4 13.3 1.0
CE1 A:PHE185 4.5 11.9 1.0
CE2 A:PHE174 4.5 8.0 1.0
CB A:TYR172 4.6 28.8 1.0
CZ A:PHE174 4.7 7.3 1.0
O A:HOH316 4.9 13.1 1.0
C A:TYR172 5.0 22.0 1.0

Zinc binding site 3 out of 4 in 1mmp

Go back to Zinc Binding Sites List in 1mmp
Zinc binding site 3 out of 4 in the Matrilysin Complexed with Carboxylate Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Matrilysin Complexed with Carboxylate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1

b:14.6
occ:1.00
O2 B:RSS269 2.0 14.1 1.0
NE2 B:HIS218 2.1 10.8 1.0
NE2 B:HIS228 2.1 12.1 1.0
NE2 B:HIS222 2.2 11.1 1.0
O1 B:RSS269 2.7 11.5 1.0
C1 B:RSS269 2.7 12.0 1.0
CE1 B:HIS228 3.0 11.8 1.0
CD2 B:HIS218 3.1 11.4 1.0
CD2 B:HIS222 3.1 12.6 1.0
CE1 B:HIS218 3.1 12.5 1.0
CE1 B:HIS222 3.1 10.2 1.0
CD2 B:HIS228 3.1 10.2 1.0
ND1 B:HIS228 4.1 10.7 1.0
C2 B:RSS269 4.1 11.1 1.0
O B:HOH353 4.2 21.7 1.0
CG B:HIS228 4.2 11.6 1.0
O B:HOH352 4.2 18.6 1.0
CG B:HIS218 4.2 9.2 1.0
ND1 B:HIS218 4.2 10.4 1.0
ND1 B:HIS222 4.2 10.6 1.0
CG B:HIS222 4.2 11.2 1.0
C3 B:RSS269 4.5 10.1 1.0
CE B:MET236 4.6 8.8 1.0
OE2 B:GLU219 4.7 14.2 1.0
C13 B:RSS269 4.9 7.2 1.0
OE1 B:GLU219 4.9 10.1 1.0

Zinc binding site 4 out of 4 in 1mmp

Go back to Zinc Binding Sites List in 1mmp
Zinc binding site 4 out of 4 in the Matrilysin Complexed with Carboxylate Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Matrilysin Complexed with Carboxylate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2

b:12.4
occ:1.00
NE2 B:HIS168 2.0 11.4 1.0
OD2 B:ASP170 2.0 28.4 1.0
NE2 B:HIS183 2.1 13.2 1.0
ND1 B:HIS196 2.2 12.7 1.0
CG B:ASP170 2.7 27.3 1.0
OD1 B:ASP170 2.7 25.7 1.0
CD2 B:HIS168 2.9 11.9 1.0
CE1 B:HIS183 3.0 11.9 1.0
CE1 B:HIS168 3.0 13.2 1.0
CE1 B:HIS196 3.0 11.9 1.0
CD2 B:HIS183 3.1 10.9 1.0
CG B:HIS196 3.2 10.8 1.0
CB B:HIS196 3.7 8.8 1.0
CB B:ASP170 4.0 27.1 1.0
O B:TYR172 4.0 22.4 1.0
CG B:HIS168 4.0 15.0 1.0
ND1 B:HIS168 4.1 15.2 1.0
ND1 B:HIS183 4.1 9.4 1.0
CG B:HIS183 4.2 10.6 1.0
NE2 B:HIS196 4.2 11.0 1.0
CD2 B:HIS196 4.4 11.4 1.0
CZ B:PHE185 4.4 9.8 1.0
CE1 B:PHE185 4.5 13.2 1.0
CB B:TYR172 4.5 29.3 1.0
CE2 B:PHE174 4.6 8.5 1.0
CZ B:PHE174 4.8 7.9 1.0
C B:TYR172 5.0 22.9 1.0
O B:HOH347 5.0 11.8 1.0

Reference:

M.F.Browner, W.W.Smith, A.L.Castelhano. Matrilysin-Inhibitor Complexes: Common Themes Among Metalloproteases. Biochemistry V. 34 6602 1995.
ISSN: ISSN 0006-2960
PubMed: 7756291
DOI: 10.1021/BI00020A004
Page generated: Wed Dec 16 02:57:14 2020

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