Samarium in PDB 1lt7: Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions

Enzymatic activity of Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions

All present enzymatic activity of Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions:
2.1.1.5;

Protein crystallography data

The structure of Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions, PDB code: 1lt7 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)*	9.99 / 2.15
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	109.990, 90.085, 89.085, 90.00, 122.10, 90.00
*R / R_free (%)*	20.3 / 24.9

Samarium Binding Sites:

The binding sites of Samarium atom in the Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions (pdb code 1lt7). This binding sites where shown within 5.0 Angstroms radius around Samarium atom.
In total 4 binding sites of Samarium where determined in the Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions, PDB code: 1lt7:
Jump to Samarium binding site number: 1; 2; 3; 4;

Samarium binding site 1 out of 4 in 1lt7

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Samarium Binding Sites List in 1lt7

Samarium binding site 1 out of 4 in the Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions

Mono view

Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 1 of Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Sm501 b:35.3 occ:0.80	O6	A:CIT601	2.3	34.8	0.8
	O4	A:CIT601	2.5	25.7	0.8
	O7	A:CIT601	2.6	27.7	0.8
	O	A:HOH646	2.6	37.5	1.0
	O	A:HOH618	2.8	35.9	1.0
	C6	A:CIT601	3.2	32.0	0.8
	C3	A:CIT601	3.3	28.7	0.8
	O	A:HOH688	3.5	52.2	1.0
	C5	A:CIT601	3.5	24.3	0.8
	C4	A:CIT601	3.9	26.8	0.8
	NZ	A:LYS283	4.3	36.9	1.0
	O5	A:CIT601	4.3	32.5	0.8
	O	A:HOH707	4.4	52.3	1.0
	O2	A:CIT601	4.5	29.0	0.8
	O	A:HOH647	4.6	34.5	1.0
	OG1	A:THR222	4.7	23.1	1.0
	O3	A:CIT601	4.7	25.9	0.8
	C2	A:CIT601	4.7	29.1	0.8
	CG2	A:THR222	4.8	20.3	1.0
	O	A:HOH614	5.0	37.5	1.0

Samarium binding site 2 out of 4 in 1lt7

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Samarium Binding Sites List in 1lt7

Samarium binding site 2 out of 4 in the Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions

Mono view

Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 2 of Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Sm503 b:53.6 occ:0.30	O	A:HOH749	2.6	69.3	1.0
A:Sm503 b:53.6 occ:0.30	NH1	A:ARG65	4.2	45.4	1.0

Samarium binding site 3 out of 4 in 1lt7

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Samarium Binding Sites List in 1lt7

Samarium binding site 3 out of 4 in the Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions

Mono view

Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 3 of Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Sm502 b:46.3 occ:0.50	O	B:HOH702	2.1	50.8	1.0
	O	A:HOH694	2.7	45.5	1.0
	NH2	B:ARG65	3.9	45.2	1.0
	NE2	A:HIS52	4.6	38.7	1.0
	CZ	B:ARG65	5.0	43.7	1.0

Samarium binding site 4 out of 4 in 1lt7

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Samarium Binding Sites List in 1lt7

Samarium binding site 4 out of 4 in the Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions

Mono view

Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 4 of Oxidized Homo Sapiens Betaine-Homocysteine S-Methyltransferase in Complex with Four Sm(III) Ions within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Sm504 b:49.9 occ:0.30	C2	B:CIT602	2.7	33.5	0.8
	O2	B:CIT602	3.2	35.6	0.8
	C1	B:CIT602	3.4	35.0	0.8
	C3	B:CIT602	3.6	34.3	0.8
	C4	B:CIT602	3.7	33.0	0.8
	O7	B:CIT602	3.9	34.6	0.8
	O1	B:CIT602	4.5	35.9	0.8
	OG1	B:THR222	4.7	26.6	1.0
	CG2	B:THR222	4.8	25.9	1.0

Reference:

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

Page generated: Thu Oct 10 13:47:29 2024

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