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Zinc in PDB 1bll: X-Ray Crystallographic Determination of the Structure of Bovine Lens Leucine Aminopeptidase Complexed with Amastatin: Formulation of A Catalytic Mechanism Featuring A Gem-Diolate Transition State

Enzymatic activity of X-Ray Crystallographic Determination of the Structure of Bovine Lens Leucine Aminopeptidase Complexed with Amastatin: Formulation of A Catalytic Mechanism Featuring A Gem-Diolate Transition State

All present enzymatic activity of X-Ray Crystallographic Determination of the Structure of Bovine Lens Leucine Aminopeptidase Complexed with Amastatin: Formulation of A Catalytic Mechanism Featuring A Gem-Diolate Transition State:
3.4.11.1;

Protein crystallography data

The structure of X-Ray Crystallographic Determination of the Structure of Bovine Lens Leucine Aminopeptidase Complexed with Amastatin: Formulation of A Catalytic Mechanism Featuring A Gem-Diolate Transition State, PDB code: 1bll was solved by H.Kim, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.40
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 130.300, 130.300, 121.900, 90.00, 90.00, 120.00
R / Rfree (%) 19.8 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the X-Ray Crystallographic Determination of the Structure of Bovine Lens Leucine Aminopeptidase Complexed with Amastatin: Formulation of A Catalytic Mechanism Featuring A Gem-Diolate Transition State (pdb code 1bll). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the X-Ray Crystallographic Determination of the Structure of Bovine Lens Leucine Aminopeptidase Complexed with Amastatin: Formulation of A Catalytic Mechanism Featuring A Gem-Diolate Transition State, PDB code: 1bll:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1bll

Go back to Zinc Binding Sites List in 1bll
Zinc binding site 1 out of 2 in the X-Ray Crystallographic Determination of the Structure of Bovine Lens Leucine Aminopeptidase Complexed with Amastatin: Formulation of A Catalytic Mechanism Featuring A Gem-Diolate Transition State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Crystallographic Determination of the Structure of Bovine Lens Leucine Aminopeptidase Complexed with Amastatin: Formulation of A Catalytic Mechanism Featuring A Gem-Diolate Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn488

b:9.1
occ:1.00
 O1 I:L2O2 2.1 20.2 1.0
OD1 E:ASP332 2.2 7.4 1.0
OE1 E:GLU334 2.2 12.0 1.0
OD2 E:ASP255 2.2 12.9 1.0
O E:ASP332 2.4 9.8 1.0
OD1 E:ASP255 2.9 2.0 1.0
CG E:ASP255 2.9 6.1 1.0
C E:ASP332 2.9 4.2 1.0
CD E:GLU334 3.0 9.8 1.0
CG E:ASP332 3.1 8.5 1.0
OE2 E:GLU334 3.2 6.7 1.0
C6 I:L2O2 3.2 29.8 1.0
CA E:ASP332 3.2 4.5 1.0
ZN E:ZN489 3.3 17.4 1.0
C I:L2O2 3.5 20.0 1.0
CB E:ASP332 3.6 7.0 1.0
O I:L2O2 3.9 16.9 1.0
N I:VAL3 4.0 20.2 1.0
N E:ALA333 4.0 6.3 1.0
OD2 E:ASP332 4.1 5.9 1.0
C1 I:L2O2 4.2 13.5 1.0
N E:GLU334 4.3 2.5 1.0
NZ E:LYS262 4.3 2.0 1.0
N I:L2O2 4.3 20.7 1.0
CB E:ASP255 4.4 2.0 1.0
CG E:GLU334 4.4 8.2 1.0
OD1 E:ASN305 4.5 5.0 1.0
CE E:LYS262 4.5 2.0 1.0
CA E:ALA333 4.5 5.0 1.0
N E:ASP332 4.6 5.2 1.0
NH2 E:ARG336 4.7 10.7 1.0
CA E:GLY257 4.7 4.0 1.0
CA I:VAL3 4.9 19.4 1.0
O E:THR331 4.9 5.2 1.0
CB E:GLU334 4.9 5.7 1.0
NH1 E:ARG336 5.0 6.5 1.0
C E:ALA333 5.0 3.9 1.0

Zinc binding site 2 out of 2 in 1bll

Go back to Zinc Binding Sites List in 1bll
Zinc binding site 2 out of 2 in the X-Ray Crystallographic Determination of the Structure of Bovine Lens Leucine Aminopeptidase Complexed with Amastatin: Formulation of A Catalytic Mechanism Featuring A Gem-Diolate Transition State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of X-Ray Crystallographic Determination of the Structure of Bovine Lens Leucine Aminopeptidase Complexed with Amastatin: Formulation of A Catalytic Mechanism Featuring A Gem-Diolate Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn489

b:17.4
occ:1.00
 N I:L2O2 2.1 20.7 1.0
O1 I:L2O2 2.2 20.2 1.0
OD2 E:ASP273 2.2 7.0 1.0
OE2 E:GLU334 2.2 6.7 1.0
OD2 E:ASP255 2.2 12.9 1.0
NZ E:LYS250 2.3 10.5 1.0
CG E:ASP273 3.0 4.7 1.0
C6 I:L2O2 3.1 29.8 1.0
C1 I:L2O2 3.1 13.5 1.0
CG E:ASP255 3.1 6.1 1.0
OD1 E:ASP273 3.2 8.4 1.0
ZN E:ZN488 3.3 9.1 1.0
CD E:GLU334 3.3 9.8 1.0
OE1 E:GLU334 3.7 12.0 1.0
CE E:LYS250 3.8 6.0 1.0
CB E:ASP255 3.8 2.0 1.0
O E:THR359 4.0 11.2 1.0
OD1 E:ASP255 4.1 2.0 1.0
C2 I:L2O2 4.2 20.2 1.0
CE E:MET270 4.3 15.1 1.0
C I:L2O2 4.4 20.0 1.0
CB E:ASP273 4.4 4.3 1.0
CD E:LYS250 4.5 2.0 1.0
NH1 E:ARG336 4.5 6.5 1.0
CG E:GLU334 4.6 8.2 1.0
CG1 E:ILE252 4.7 2.0 1.0
N E:GLY335 4.8 5.7 1.0
CB E:ILE252 4.9 4.0 1.0
CG2 E:ILE252 5.0 2.0 1.0
O I:L2O2 5.0 16.9 1.0
O E:LEU360 5.0 6.6 1.0

Reference:

H.Kim, W.N.Lipscomb. X-Ray Crystallographic Determination of the Structure of Bovine Lens Leucine Aminopeptidase Complexed with Amastatin: Formulation of A Catalytic Mechanism Featuring A Gem-Diolate Transition State. Biochemistry V. 32 8465 1993.
ISSN: ISSN 0006-2960
PubMed: 8357796
DOI: 10.1021/BI00084A011
Page generated: Wed Dec 16 02:45:52 2020

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