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Zinc in PDB 3oho: Catalytic Domain of Stromelysin-1 in Complex with N-Hydroxy-2-(4- Methylphenylsulfonamido)Acetamide

Enzymatic activity of Catalytic Domain of Stromelysin-1 in Complex with N-Hydroxy-2-(4- Methylphenylsulfonamido)Acetamide

All present enzymatic activity of Catalytic Domain of Stromelysin-1 in Complex with N-Hydroxy-2-(4- Methylphenylsulfonamido)Acetamide:
3.4.24.17;

Protein crystallography data

The structure of Catalytic Domain of Stromelysin-1 in Complex with N-Hydroxy-2-(4- Methylphenylsulfonamido)Acetamide, PDB code: 3oho was solved by T.Kowatz, J.H.Naismith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.60 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 56.482, 121.044, 46.872, 90.00, 90.00, 90.00
R / Rfree (%) 25.5 / 26.4

Other elements in 3oho:

The structure of Catalytic Domain of Stromelysin-1 in Complex with N-Hydroxy-2-(4- Methylphenylsulfonamido)Acetamide also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Catalytic Domain of Stromelysin-1 in Complex with N-Hydroxy-2-(4- Methylphenylsulfonamido)Acetamide (pdb code 3oho). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Catalytic Domain of Stromelysin-1 in Complex with N-Hydroxy-2-(4- Methylphenylsulfonamido)Acetamide, PDB code: 3oho:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3oho

Go back to Zinc Binding Sites List in 3oho
Zinc binding site 1 out of 2 in the Catalytic Domain of Stromelysin-1 in Complex with N-Hydroxy-2-(4- Methylphenylsulfonamido)Acetamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Catalytic Domain of Stromelysin-1 in Complex with N-Hydroxy-2-(4- Methylphenylsulfonamido)Acetamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn4

b:51.5
occ:1.00
OD2 A:ASP153 2.0 47.3 1.0
NE2 A:HIS151 2.1 47.6 1.0
NE2 A:HIS166 2.1 50.4 1.0
ND1 A:HIS179 2.1 45.5 1.0
CE1 A:HIS166 2.9 51.1 1.0
CD2 A:HIS151 3.0 46.6 1.0
CG A:ASP153 3.0 48.7 1.0
CE1 A:HIS179 3.1 45.2 1.0
CE1 A:HIS151 3.1 47.9 1.0
CG A:HIS179 3.1 44.4 1.0
CD2 A:HIS166 3.2 51.0 1.0
OD1 A:ASP153 3.4 50.1 1.0
CB A:HIS179 3.5 44.1 1.0
ND1 A:HIS166 4.1 52.3 1.0
CG A:HIS151 4.2 47.0 1.0
ND1 A:HIS151 4.2 48.2 1.0
NE2 A:HIS179 4.2 44.6 1.0
CG A:HIS166 4.2 51.9 1.0
CD2 A:HIS179 4.2 44.4 1.0
O A:TYR155 4.2 51.7 1.0
CB A:ASP153 4.4 49.6 1.0
OH A:TYR168 4.4 53.0 1.0
CZ A:PHE157 4.5 50.6 1.0
CE1 A:TYR168 4.5 51.3 1.0
CE2 A:PHE157 4.5 49.6 1.0
CA A:HIS179 4.9 44.4 1.0
CZ A:TYR168 4.9 53.0 1.0

Zinc binding site 2 out of 2 in 3oho

Go back to Zinc Binding Sites List in 3oho
Zinc binding site 2 out of 2 in the Catalytic Domain of Stromelysin-1 in Complex with N-Hydroxy-2-(4- Methylphenylsulfonamido)Acetamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Catalytic Domain of Stromelysin-1 in Complex with N-Hydroxy-2-(4- Methylphenylsulfonamido)Acetamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn5

b:70.9
occ:1.00
O5 A:Z79252 2.0 51.4 1.0
O4 A:Z79252 2.0 57.7 1.0
NE2 A:HIS211 2.1 87.8 1.0
NE2 A:HIS205 2.1 79.9 1.0
NE2 A:HIS201 2.1 80.3 1.0
C8 A:Z79252 2.7 58.2 1.0
N2 A:Z79252 2.8 54.4 1.0
CD2 A:HIS201 3.0 75.6 1.0
CE1 A:HIS205 3.0 82.3 1.0
CD2 A:HIS211 3.0 90.9 1.0
CE1 A:HIS211 3.2 89.5 1.0
CD2 A:HIS205 3.2 75.4 1.0
CE1 A:HIS201 3.2 83.2 1.0
CG A:HIS201 4.1 76.3 1.0
ND1 A:HIS205 4.2 80.6 1.0
CG A:HIS211 4.2 95.8 1.0
C7 A:Z79252 4.2 63.3 1.0
ND1 A:HIS201 4.2 81.4 1.0
ND1 A:HIS211 4.2 94.8 1.0
CG A:HIS205 4.3 75.9 1.0
OE2 A:GLU202 4.3 63.6 1.0
N1 A:Z79252 4.8 66.7 1.0
C6 A:Z79252 4.9 60.1 1.0
OE1 A:GLU202 4.9 61.4 1.0
CE A:MET219 5.0 74.9 1.0
CD A:GLU202 5.0 61.9 1.0

Reference:

T.Kowatz, J.H.Naismith. Non-Resonance Raman Difference Spectroscopy As A Tool to Probe Enthalpy-Entropy Compensation and the Interfacial Mobility Model To Be Published.
Page generated: Wed Dec 16 04:40:23 2020

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