Zinc in PDB 1lt8: Reduced Homo Sapiens Betaine-Homocysteine S- Methyltransferase in Complex with S-(Delta-Carboxybutyl)-L- Homocysteine

All present enzymatic activity of Reduced Homo Sapiens Betaine-Homocysteine S- Methyltransferase in Complex with S-(Delta-Carboxybutyl)-L- Homocysteine:
2.1.1.5;

The structure of Reduced Homo Sapiens Betaine-Homocysteine S- Methyltransferase in Complex with S-(Delta-Carboxybutyl)-L- Homocysteine, PDB code: 1lt8 was solved by J.C.Evans, D.P.Huddler, J.Jiracek, C.Castro, N.S.Millian, T.A.Garrow, M.L.Ludwig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.05
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	109.702, 90.836, 88.403, 90.00, 122.28, 90.00
R / Rfree (%)	22.6 / 25.5

The binding sites of Zinc atom in the Reduced Homo Sapiens Betaine-Homocysteine S- Methyltransferase in Complex with S-(Delta-Carboxybutyl)-L- Homocysteine (pdb code 1lt8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Reduced Homo Sapiens Betaine-Homocysteine S- Methyltransferase in Complex with S-(Delta-Carboxybutyl)-L- Homocysteine, PDB code: 1lt8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Reduced Homo Sapiens Betaine-Homocysteine S- Methyltransferase in Complex with S-(Delta-Carboxybutyl)-L- Homocysteine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Reduced Homo Sapiens Betaine-Homocysteine S- Methyltransferase in Complex with S-(Delta-Carboxybutyl)-L- Homocysteine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:24.0 occ:0.90 SG A:CYS300 2.3 28.2 1.0 S18 A:CBH601 2.3 32.8 0.9 SG A:CYS217 2.3 26.4 1.0 SG A:CYS299 2.3 29.4 1.0 C19 A:CBH601 3.2 35.3 0.9 CB A:CYS217 3.2 27.1 1.0 C17 A:CBH601 3.4 34.3 0.9 N A:CYS300 3.5 22.6 1.0 CB A:CYS300 3.6 23.0 1.0 CB A:CYS299 3.7 27.2 1.0 C20 A:CBH601 3.8 36.1 0.9 C16 A:CBH601 4.0 34.3 0.9 CA A:CYS300 4.1 22.2 1.0 CA A:CYS217 4.1 26.4 1.0 O A:HOH858 4.3 77.9 1.0 CD2 A:LEU249 4.5 21.6 1.0 C A:CYS299 4.5 24.1 1.0 CA A:CYS299 4.6 25.5 1.0 O A:HOH873 4.7 99.3 1.0 CE2 A:TYR160 4.7 42.0 1.0 CD2 A:TYR160 4.8 41.6 1.0 ND2 A:ASN216 4.8 28.8 1.0 O A:HOH708 4.8 20.0 1.0 N A:CYS217 4.9 27.4 1.0

Zinc binding site 2 out of 2 in the Reduced Homo Sapiens Betaine-Homocysteine S- Methyltransferase in Complex with S-(Delta-Carboxybutyl)-L- Homocysteine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Reduced Homo Sapiens Betaine-Homocysteine S- Methyltransferase in Complex with S-(Delta-Carboxybutyl)-L- Homocysteine within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:30.5 occ:0.75 SG B:CYS299 2.3 35.0 1.0 SG B:CYS300 2.3 31.0 1.0 SG B:CYS217 2.3 32.5 1.0 S18 B:CBH602 2.3 37.9 0.8 C19 B:CBH602 3.1 41.0 0.8 CB B:CYS217 3.2 31.5 1.0 C17 B:CBH602 3.5 36.9 0.8 CB B:CYS300 3.5 30.2 1.0 O B:HOH864 3.5 85.7 1.0 N B:CYS300 3.5 28.9 1.0 C20 B:CBH602 3.6 42.1 0.8 CB B:CYS299 3.8 32.9 1.0 C16 B:CBH602 4.0 37.2 0.8 CA B:CYS217 4.1 30.9 1.0 CA B:CYS300 4.1 29.6 1.0 CD2 B:LEU249 4.4 25.9 1.0 C B:CYS299 4.6 29.9 1.0 CD2 B:TYR160 4.6 50.4 1.0 CE2 B:TYR160 4.7 50.3 1.0 CA B:CYS299 4.7 30.4 1.0 O B:HOH714 4.7 31.8 1.0 N B:CYS217 4.7 30.0 1.0 C21 B:CBH602 4.9 42.0 0.8

J.C.Evans, D.P.Huddler, J.Jiracek, C.Castro, N.S.Millian, T.A.Garrow, M.L.Ludwig. Betaine-Homocysteine Methyltransferase: Zinc in A Distorted Barrel. Structure V. 10 1159 2002.
ISSN: ISSN 0969-2126
PubMed: 12220488
DOI: 10.1016/S0969-2126(02)00796-7