Zinc in PDB 1d1t: Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141

All present enzymatic activity of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141:
1.1.1.1;

The structure of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141, PDB code: 1d1t was solved by P.T.Xie, T.D.Hurley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	85.900, 90.500, 119.800, 90.00, 99.30, 90.00
R / Rfree (%)	21.6 / 27.4

The structure of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 also contains other interesting chemical elements:

Arsenic

(As)

5 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 19;

Binding sites:

The binding sites of Zinc atom in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 (pdb code 1d1t). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 19 binding sites of Zinc where determined in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141, PDB code: 1d1t:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 19 in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn375 b:49.6 occ:1.00 SG A:CYS103 2.1 45.0 1.0 SG A:CYS111 2.3 49.7 1.0 SG A:CYS97 2.4 54.8 1.0 SG A:CYS100 2.4 51.2 1.0 CB A:CYS111 3.1 46.2 1.0 CB A:CYS103 3.2 42.7 1.0 CB A:CYS97 3.4 47.8 1.0 N A:CYS97 3.4 45.2 1.0 CB A:CYS100 3.5 48.2 1.0 CA A:CYS111 3.6 47.1 1.0 N A:ILE112 3.7 48.9 1.0 N A:ARG98 3.8 47.9 1.0 N A:CYS100 3.8 49.5 1.0 CA A:CYS97 3.8 45.8 1.0 C A:CYS111 4.2 47.7 1.0 CA A:CYS100 4.2 47.6 1.0 C A:CYS97 4.2 46.9 1.0 CA A:CYS103 4.3 40.4 1.0 N A:CYS103 4.3 39.1 1.0 N A:GLU99 4.3 48.6 1.0 CG2 A:ILE112 4.4 46.6 1.0 C A:GLN96 4.4 43.3 1.0 CA A:GLN96 4.6 40.2 1.0 CA A:ARG98 4.7 48.0 1.0 C A:CYS100 4.8 47.7 1.0 N A:CYS111 4.9 45.9 1.0 CA A:ILE112 4.9 49.4 1.0 O A:CYS100 4.9 47.0 1.0 C A:GLU99 4.9 51.4 1.0 CB A:ILE112 4.9 48.1 1.0 C A:ARG98 5.0 48.0 1.0

Zinc binding site 2 out of 19 in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn376 b:35.6 occ:1.00 SG A:CYS174 2.0 34.6 1.0 NE2 A:HIS67 2.1 32.5 1.0 O A:ACT501 2.2 40.1 1.0 SG A:CYS46 2.3 38.5 1.0 CD2 A:HIS67 3.1 31.4 1.0 CB A:CYS46 3.1 38.9 1.0 CE1 A:HIS67 3.2 31.3 1.0 C A:ACT501 3.4 39.1 1.0 CB A:CYS174 3.4 32.0 1.0 C5N A:NAD1377 3.7 26.5 1.0 OG1 A:THR48 4.0 38.2 1.0 CH3 A:ACT501 4.0 37.6 1.0 CB A:THR48 4.2 37.9 1.0 C6N A:NAD1377 4.2 24.9 1.0 CG A:HIS67 4.3 31.0 1.0 C4N A:NAD1377 4.3 28.9 1.0 ND1 A:HIS67 4.3 31.2 1.0 OXT A:ACT501 4.3 41.0 1.0 CA A:CYS46 4.6 39.8 1.0 NH1 A:ARG369 4.7 33.6 1.0 CA A:CYS174 4.7 30.6 1.0 OE2 A:GLU68 4.7 43.7 1.0 N A:GLY175 4.7 34.1 1.0 N A:THR48 5.0 37.4 1.0

Zinc binding site 3 out of 19 in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:48.2 occ:1.00 OXT A:ACT504 2.1 19.5 1.0 N7A A:NAD1377 2.2 29.1 1.0 NE2 A:HIS271 2.2 44.4 1.0 O A:HOH749 2.4 43.5 1.0 CD2 A:HIS271 2.8 44.8 1.0 C A:ACT504 3.1 15.3 1.0 C8A A:NAD1377 3.1 29.8 1.0 CE1 A:HIS271 3.3 43.6 1.0 C5A A:NAD1377 3.3 31.5 1.0 O A:ACT504 3.4 19.6 1.0 N6A A:NAD1377 3.6 28.9 1.0 C6A A:NAD1377 3.9 30.2 1.0 CG A:HIS271 4.1 41.5 1.0 ND1 A:HIS271 4.3 43.1 1.0 N9A A:NAD1377 4.4 29.4 1.0 C4A A:NAD1377 4.4 31.3 1.0 CH3 A:ACT504 4.4 18.9 1.0 CG2 A:ILE269 4.5 24.1 1.0 CD1 A:LEU224 4.8 28.9 1.0

Zinc binding site 4 out of 19 in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:50.9 occ:0.50 NE2 A:HIS138 2.0 55.3 1.0 OXT A:ACT513 2.0 52.9 0.5 O A:ACT513 2.0 52.8 0.5 OXT A:ACT502 2.2 50.8 0.5 C A:ACT513 2.3 53.2 0.5 O A:ACT502 2.4 51.6 0.5 C A:ACT502 2.6 51.5 0.5 CE1 A:HIS138 2.8 52.8 1.0 CD2 A:HIS138 3.1 55.8 1.0 CH3 A:ACT513 3.8 54.2 0.5 ND1 A:HIS138 4.0 53.5 1.0 CH3 A:ACT502 4.1 51.7 0.5 CG A:HIS138 4.1 54.6 1.0 CD A:LYS60 4.4 63.0 1.0

Zinc binding site 5 out of 19 in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:49.2 occ:1.00 OXT B:ACT507 1.8 29.1 1.0 N7A B:NAD2377 1.9 23.2 1.0 O B:HOH735 1.9 44.9 1.0 NE2 B:HIS271 2.1 41.5 1.0 N6A B:NAD2377 2.8 25.9 1.0 C B:ACT507 2.9 24.5 1.0 CD2 B:HIS271 2.9 38.3 1.0 C5A B:NAD2377 3.0 20.6 1.0 C8A B:NAD2377 3.0 25.7 1.0 CE1 B:HIS271 3.2 39.3 1.0 C6A B:NAD2377 3.4 25.8 1.0 O B:ACT507 3.5 25.7 1.0 CH3 B:ACT507 4.1 23.2 1.0 CG B:HIS271 4.1 38.9 1.0 C4A B:NAD2377 4.1 23.2 1.0 N9A B:NAD2377 4.2 23.9 1.0 ND1 B:HIS271 4.2 39.9 1.0 CG2 B:ILE269 4.3 25.5 1.0 N1A B:NAD2377 4.8 22.7 1.0 CD1 B:LEU224 4.9 30.1 1.0

Zinc binding site 6 out of 19 in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn408 b:47.2 occ:1.00 OE2 A:GLU360 1.9 45.9 1.0 O A:HOH793 2.0 31.4 1.0 OE2 A:GLU357 2.0 19.8 1.0 OE1 A:GLU357 2.4 23.0 1.0 CD A:GLU357 2.5 24.7 1.0 CD A:GLU360 3.1 48.8 1.0 OE1 A:GLU360 3.9 49.6 1.0 CD2 A:LEU361 4.0 26.5 1.0 CG A:GLU360 4.0 45.6 1.0 CG A:GLU357 4.0 27.9 1.0 O A:HOH727 4.3 40.0 1.0 CB A:GLU360 4.4 42.2 1.0 CG A:LEU361 4.5 33.6 1.0 O A:GLU357 4.9 35.4 1.0 CB A:GLU357 5.0 32.3 1.0

Zinc binding site 7 out of 19 in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn375 b:28.7 occ:1.00 SG B:CYS97 2.0 25.0 1.0 SG B:CYS111 2.2 24.5 1.0 SG B:CYS103 2.3 19.3 1.0 SG B:CYS100 2.6 24.9 1.0 CB B:CYS111 3.1 28.4 1.0 CB B:CYS97 3.3 27.1 1.0 CB B:CYS103 3.4 23.5 1.0 N B:CYS97 3.4 23.4 1.0 CB B:CYS100 3.5 20.1 1.0 CA B:CYS111 3.6 26.5 1.0 CA B:CYS97 3.8 23.0 1.0 N B:ARG98 3.9 24.2 1.0 N B:CYS100 3.9 25.4 1.0 N B:ILE112 3.9 26.2 1.0 C B:CYS97 4.2 21.8 1.0 C B:CYS111 4.2 25.1 1.0 CA B:CYS100 4.3 24.2 1.0 CG1 B:ILE112 4.3 25.3 1.0 C B:GLN96 4.4 20.5 1.0 N B:GLU99 4.5 26.0 1.0 CA B:CYS103 4.5 24.9 1.0 N B:CYS103 4.5 22.6 1.0 CA B:GLN96 4.6 18.8 1.0 N B:CYS111 4.8 26.2 1.0 CA B:ARG98 4.9 25.6 1.0 C B:CYS100 4.9 25.6 1.0 O B:CYS100 5.0 29.1 1.0

Zinc binding site 8 out of 19 in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn376 b:28.1 occ:1.00 NE2 B:HIS67 2.1 9.7 1.0 SG B:CYS174 2.2 19.1 1.0 SG B:CYS46 2.3 30.5 1.0 OXT B:ACT506 2.7 27.1 1.0 CE1 B:HIS67 2.9 5.5 1.0 CB B:CYS46 3.2 31.9 1.0 CD2 B:HIS67 3.2 12.0 1.0 C B:ACT506 3.4 26.1 1.0 CB B:CYS174 3.5 21.0 1.0 CH3 B:ACT506 3.5 12.1 1.0 C5N B:NAD2377 3.6 15.2 1.0 OG1 B:THR48 3.9 30.0 1.0 ND1 B:HIS67 4.1 7.6 1.0 C6N B:NAD2377 4.2 17.8 1.0 CB B:THR48 4.2 27.4 1.0 C4N B:NAD2377 4.3 18.1 1.0 CG B:HIS67 4.3 10.6 1.0 O B:ACT506 4.5 37.2 1.0 NH2 B:ARG369 4.5 29.5 1.0 OE2 B:GLU68 4.6 35.1 1.0 CA B:CYS46 4.6 29.2 1.0 N B:GLY175 4.6 27.3 1.0 CA B:CYS174 4.8 22.6 1.0

Zinc binding site 9 out of 19 in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn404 b:31.4 occ:1.00 O B:HOH725 1.8 11.9 1.0 NE2 B:HIS138 2.0 18.1 1.0 CE1 B:HIS138 2.7 18.3 1.0 CD2 B:HIS138 3.2 23.1 1.0 ND1 B:HIS138 3.9 20.9 1.0 O B:HOH649 3.9 31.6 1.0 CG B:HIS138 4.2 23.1 1.0 O B:PHE61 4.5 30.6 1.0 C2 B:CAC991 4.8 32.2 1.0 CD B:LYS60 4.9 42.3 1.0 CB B:LYS60 4.9 29.7 1.0

Zinc binding site 10 out of 19 in the Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Mutant of Human Sigma Alcohol Dehydrogenase with Leucine at Position 141 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn405 b:51.8 occ:1.00 OE1 D:GLU99 2.1 30.2 1.0 OD1 B:ASP341 2.4 46.8 1.0 O D:ACT509 2.5 18.3 1.0 OE2 D:GLU99 2.6 32.3 1.0 CD D:GLU99 2.7 30.6 1.0 OXT D:ACT509 2.7 20.2 1.0 CG B:ASP341 2.9 44.3 1.0 C D:ACT509 2.9 17.0 1.0 O D:ACT508 2.9 31.1 1.0 OD2 B:ASP341 2.9 45.5 1.0 OXT D:ACT508 3.3 25.1 1.0 C D:ACT508 3.3 26.3 1.0 CG D:GLU99 4.2 28.3 1.0 CB B:ASP341 4.2 41.7 1.0 CH3 D:ACT509 4.4 20.3 1.0 CH3 D:ACT508 4.6 23.1 1.0 O B:HOH842 4.6 43.5 1.0 CG B:GLN344 4.7 38.9 1.0 CB D:GLU99 4.8 27.9 1.0 CB B:ASP343 4.9 34.5 1.0

P.T.Xie, T.D.Hurley. Methionine-141 Directly Influences the Binding of 4-Methylpyrazole in Human Sigma Sigma Alcohol Dehydrogenase. Protein Sci. V. 8 2639 1999.
ISSN: ISSN 0961-8368
PubMed: 10631979