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Zinc in PDB 1sln: Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with the N-Carboxy-Alkyl Inhibitor L-702,842

Enzymatic activity of Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with the N-Carboxy-Alkyl Inhibitor L-702,842

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with the N-Carboxy-Alkyl Inhibitor L-702,842:
3.4.24.17;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with the N-Carboxy-Alkyl Inhibitor L-702,842, PDB code: 1sln was solved by J.W.Becker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.27
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 47.230, 47.230, 150.850, 90.00, 90.00, 120.00
R / Rfree (%) 22.6 / 29.9

Other elements in 1sln:

The structure of Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with the N-Carboxy-Alkyl Inhibitor L-702,842 also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with the N-Carboxy-Alkyl Inhibitor L-702,842 (pdb code 1sln). 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 Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with the N-Carboxy-Alkyl Inhibitor L-702,842, PDB code: 1sln:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1sln

Go back to Zinc Binding Sites List in 1sln
Zinc binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with the N-Carboxy-Alkyl Inhibitor L-702,842


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with the N-Carboxy-Alkyl Inhibitor L-702,842 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn257

b:9.2
occ:1.00
NE2 A:HIS211 1.7 7.4 1.0
O5 A:INH256 1.7 7.9 1.0
NE2 A:HIS201 1.8 6.4 1.0
NE2 A:HIS205 1.9 5.3 1.0
CE1 A:HIS211 2.7 7.5 1.0
C3 A:INH256 2.7 5.2 1.0
CD2 A:HIS211 2.8 8.4 1.0
CD2 A:HIS201 2.8 7.2 1.0
CE1 A:HIS201 2.8 8.9 1.0
CE1 A:HIS205 2.8 5.0 1.0
CD2 A:HIS205 3.0 4.1 1.0
O4 A:INH256 3.0 7.4 1.0
ND1 A:HIS211 3.8 8.6 1.0
CG A:HIS211 3.9 8.0 1.0
ND1 A:HIS201 3.9 6.0 1.0
CG A:HIS201 4.0 7.5 1.0
ND1 A:HIS205 4.0 2.7 1.0
C2 A:INH256 4.1 4.5 1.0
CG A:HIS205 4.1 5.2 1.0
H70 A:INH256 4.3 0.0 1.0
O A:HOH301 4.4 4.8 1.0
C8 A:INH256 4.4 5.8 1.0
C7 A:INH256 4.4 7.2 1.0
N6 A:INH256 4.5 3.6 1.0
OE1 A:GLU202 4.6 15.2 1.0
HD1 A:HIS211 4.7 0.0 1.0
HD1 A:HIS201 4.8 0.0 1.0
CE A:MET219 4.9 3.7 1.0
HD1 A:HIS205 4.9 0.0 1.0
H2 A:HOH301 4.9 0.0 1.0
O A:PRO221 4.9 7.8 1.0
OE2 A:GLU202 4.9 15.8 1.0
O A:MET219 5.0 5.6 1.0

Zinc binding site 2 out of 2 in 1sln

Go back to Zinc Binding Sites List in 1sln
Zinc binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with the N-Carboxy-Alkyl Inhibitor L-702,842


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Catalytic Domain of Human Fibroblast Stromelysin-1 Inhibited with the N-Carboxy-Alkyl Inhibitor L-702,842 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn258

b:13.2
occ:1.00
NE2 A:HIS151 1.8 10.0 1.0
NE2 A:HIS166 1.8 17.1 1.0
OD2 A:ASP153 1.9 4.4 1.0
ND1 A:HIS179 2.1 2.1 1.0
CE1 A:HIS166 2.7 13.5 1.0
CE1 A:HIS151 2.8 9.2 1.0
CD2 A:HIS151 2.8 9.2 1.0
CG A:ASP153 2.9 8.6 1.0
CD2 A:HIS166 2.9 14.0 1.0
CG A:HIS179 3.1 3.2 1.0
CE1 A:HIS179 3.1 4.2 1.0
OD1 A:ASP153 3.4 7.3 1.0
CB A:HIS179 3.4 4.3 1.0
OH A:TYR168 3.8 12.9 1.0
HH A:TYR168 3.9 0.0 1.0
ND1 A:HIS166 3.9 11.1 1.0
ND1 A:HIS151 3.9 5.5 1.0
CG A:HIS151 4.0 7.7 1.0
CG A:HIS166 4.0 10.7 1.0
O A:TYR155 4.0 10.9 1.0
CB A:ASP153 4.1 7.7 1.0
NE2 A:HIS179 4.2 2.1 1.0
CD2 A:HIS179 4.2 2.0 1.0
CE2 A:PHE157 4.5 9.3 1.0
CE1 A:TYR168 4.6 15.8 1.0
CZ A:PHE157 4.6 9.4 1.0
CZ A:TYR168 4.7 16.5 1.0
HD1 A:HIS166 4.8 0.0 1.0
HD1 A:HIS151 4.8 0.0 1.0
O A:HOH336 4.9 10.0 1.0
CA A:HIS179 4.9 6.6 1.0

Reference:

J.W.Becker, A.I.Marcy, L.L.Rokosz, M.G.Axel, J.J.Burbaum, P.M.Fitzgerald, P.M.Cameron, C.K.Esser, W.K.Hagmann, J.D.Hermes, J.P.Springer. Stromelysin-1: Three-Dimensional Structure of the Inhibited Catalytic Domain and of the C-Truncated Proenzyme. Protein Sci. V. 4 1966 1995.
ISSN: ISSN 0961-8368
PubMed: 8535233
Page generated: Wed Oct 16 18:52:32 2024

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