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Zinc in PDB 6h0t: Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase

Enzymatic activity of Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase

All present enzymatic activity of Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase:
3.1.1.13; 3.1.1.3;

Protein crystallography data

The structure of Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase, PDB code: 6h0t was solved by C.Touvrey, X.Brazzolotto, F.Nachon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.93 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.274, 97.676, 109.640, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 24.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase (pdb code 6h0t). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase, PDB code: 6h0t:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Zinc binding site 1 out of 8 in 6h0t

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Zinc binding site 1 out of 8 in the Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase


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 Native Recombinant Human Bile Salt Activated Lipase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:47.5
occ:1.00
 NE2 A:HIS168 2.0 44.6 1.0
OXT A:ACT610 2.1 51.3 1.0
C A:ACT610 2.8 55.5 1.0
O A:ACT610 3.0 54.1 1.0
CD2 A:HIS168 3.0 42.4 1.0
CE1 A:HIS168 3.0 38.7 1.0
CD2 A:TYR208 4.0 48.1 1.0
ND1 A:HIS168 4.1 39.0 1.0
CG A:HIS168 4.1 39.8 1.0
CH3 A:ACT610 4.3 46.5 1.0
O A:TYR208 4.5 41.8 1.0
CE2 A:TYR208 4.7 50.4 1.0
CB A:TYR208 4.9 43.1 1.0
CG A:TYR208 4.9 46.2 1.0

Zinc binding site 2 out of 8 in 6h0t

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Zinc binding site 2 out of 8 in the Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase


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 Native Recombinant Human Bile Salt Activated Lipase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn602

b:35.4
occ:1.00
 OE1 A:GLU489 1.9 35.7 1.0
NE2 A:HIS487 2.0 33.6 1.0
O A:ACT609 2.2 41.8 1.0
OXT A:ACT609 2.4 36.9 1.0
C A:ACT609 2.6 38.0 1.0
CD A:GLU489 2.9 35.7 1.0
CD2 A:HIS487 3.0 33.1 1.0
CE1 A:HIS487 3.0 31.4 1.0
OE2 A:GLU489 3.3 37.0 1.0
ND1 A:HIS487 4.1 29.4 1.0
CG A:HIS487 4.1 28.2 1.0
CH3 A:ACT609 4.2 39.5 1.0
CG A:GLU489 4.3 35.2 1.0
CD A:PRO490 4.4 32.0 1.0
CA A:GLU489 4.4 33.4 1.0
CB A:GLU489 4.5 33.5 1.0

Zinc binding site 3 out of 8 in 6h0t

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Zinc binding site 3 out of 8 in the Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn603

b:35.0
occ:1.00
 OE2 A:GLU78 1.8 34.5 1.0
OD2 A:ASP77 2.0 34.3 1.0
CD A:GLU78 2.5 35.8 1.0
OE1 A:GLU78 2.7 37.8 1.0
CG A:ASP77 2.8 34.0 1.0
OD1 A:ASP77 2.9 33.9 1.0
CG A:GLU78 4.0 32.9 1.0
CB A:ASP77 4.2 32.7 1.0
N A:GLU78 4.5 35.9 1.0
CA A:ASP77 4.9 36.7 1.0

Zinc binding site 4 out of 8 in 6h0t

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Zinc binding site 4 out of 8 in the Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn604

b:65.0
occ:0.60
 OD2 A:ASP328 1.8 53.4 1.0
CG A:ASP328 2.7 57.3 1.0
OE1 A:GLU388 2.8 44.7 1.0
OD1 A:ASP328 3.0 57.0 1.0
OE2 A:GLU388 3.1 52.4 1.0
CZ A:PHE351 3.3 47.4 0.9
CD A:GLU388 3.3 48.6 1.0
CB A:MET281 3.5 70.1 1.0
N A:MET281 3.5 73.7 1.0
CE1 A:PHE351 4.0 49.7 0.9
CB A:ASP328 4.0 51.5 1.0
CA A:MET281 4.0 71.3 1.0
CB A:PRO280 4.2 71.6 1.0
N A:LEU282 4.2 70.7 1.0
O A:PHE324 4.2 49.5 1.0
CE2 A:PHE351 4.3 50.8 0.9
C A:PRO280 4.5 75.1 1.0
C A:MET281 4.6 74.8 1.0
CA A:PRO280 4.6 75.7 1.0
CD1 A:LEU347 4.6 47.1 1.0
CG A:MET281 4.8 73.4 1.0
CG A:GLU388 4.8 46.0 1.0
C A:PHE324 4.9 49.2 1.0
CB A:PHE324 4.9 45.9 1.0

Zinc binding site 5 out of 8 in 6h0t

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Zinc binding site 5 out of 8 in the Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn605

b:35.1
occ:0.90
 O A:ACT611 1.8 35.8 1.0
O A:HOH798 2.0 38.6 1.0
O A:HOH730 2.1 37.0 1.0
O A:HOH716 2.1 32.7 1.0
NE2 A:HIS48 2.2 38.0 1.0
C A:ACT611 2.3 37.7 1.0
OXT A:ACT611 2.4 44.9 1.0
CD2 A:HIS48 3.0 33.3 1.0
CE1 A:HIS48 3.2 40.8 1.0
OH A:TYR82 3.9 36.7 1.0
CH3 A:ACT611 3.9 42.4 1.0
CG A:HIS48 4.2 35.5 1.0
OD2 A:ASP79 4.2 36.4 1.0
OD1 A:ASP79 4.3 32.4 1.0
ND1 A:HIS48 4.3 38.1 1.0
CD A:PRO38 4.4 33.8 1.0
CB A:PRO34 4.5 35.5 1.0
O A:HOH725 4.5 33.0 1.0
CG A:PRO38 4.6 33.1 1.0
CG A:ASP79 4.7 35.9 1.0
CZ A:TYR82 4.7 37.7 1.0
CG A:PRO34 4.8 32.7 1.0

Zinc binding site 6 out of 8 in 6h0t

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Zinc binding site 6 out of 8 in the Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn606

b:82.8
occ:1.00
 OD2 A:ASP97 2.4 57.2 1.0
OD1 A:ASP97 2.7 41.5 1.0
CG A:ASP97 2.9 47.3 1.0
CB A:ASP97 4.4 45.4 1.0

Zinc binding site 7 out of 8 in 6h0t

Go back to Zinc Binding Sites List in 6h0t
Zinc binding site 7 out of 8 in the Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn607

b:67.3
occ:0.75
 OD2 A:ASP434 2.2 63.0 1.0
O A:HOH805 2.3 59.1 1.0
ND1 A:HIS322 2.3 65.2 1.0
OXT A:ACT612 2.4 74.2 1.0
O A:ACT612 2.5 73.9 1.0
C A:ACT612 2.7 73.1 1.0
CE1 A:HIS322 3.0 64.2 1.0
CG A:ASP434 3.3 50.2 1.0
CG A:HIS322 3.5 60.7 1.0
CB A:ASP434 3.7 48.8 1.0
CB A:HIS322 4.0 47.8 1.0
NE2 A:HIS322 4.2 61.4 1.0
CD1 A:ILE323 4.2 57.6 1.0
CH3 A:ACT612 4.2 73.5 1.0
OD1 A:ASP434 4.4 43.0 1.0
CD2 A:HIS322 4.4 60.5 1.0
CA A:ASP434 4.9 37.8 1.0

Zinc binding site 8 out of 8 in 6h0t

Go back to Zinc Binding Sites List in 6h0t
Zinc binding site 8 out of 8 in the Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of Native Recombinant Human Bile Salt Activated Lipase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn608

b:47.6
occ:0.56
 OG A:SER194 2.9 37.3 1.0
N A:GLY107 3.1 45.1 1.0
N A:ALA195 3.2 36.0 1.0
CB A:ALA195 3.3 38.0 1.0
N A:LEU110 3.5 49.4 1.0
N A:PHE109 3.5 44.7 1.0
CA A:GLY107 3.5 45.4 1.0
N A:ALA108 3.6 47.8 1.0
C A:GLY107 3.6 49.7 1.0
CB A:SER194 3.7 36.4 1.0
CA A:ALA195 3.8 34.7 1.0
CB A:PHE109 4.0 40.7 1.0
CA A:PHE109 4.1 47.5 1.0
CB A:LEU110 4.1 48.4 1.0
CD1 A:LEU110 4.2 45.9 1.0
C A:PHE109 4.2 47.6 1.0
C A:SER194 4.2 35.3 1.0
C A:GLY106 4.2 40.0 1.0
CA A:LEU110 4.3 51.7 1.0
O A:GLY107 4.4 56.9 1.0
CG A:LEU110 4.4 50.3 1.0
C A:ALA108 4.5 49.0 1.0
CA A:SER194 4.5 33.0 1.0
CA A:GLY106 4.5 33.5 1.0
CA A:ALA108 4.6 49.9 1.0
CZ3 A:TRP227 4.6 40.1 1.0
CG A:PHE109 4.8 43.2 1.0
C A:LEU110 4.9 53.2 1.0

Reference:

C.Touvrey, C.Courageux, V.Guillon, R.Terreux, F.Nachon, X.Brazzolotto. X-Ray Structures of Human Bile-Salt Activated Lipase Conjugated to Nerve Agents Surrogates. Toxicology V. 411 15 2019.
ISSN: ISSN 1879-3185
PubMed: 30359675
DOI: 10.1016/J.TOX.2018.10.015
Page generated: Mon Oct 28 22:17:20 2024

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