Calcium in PDB 1jom: The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase

Enzymatic activity of The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase

All present enzymatic activity of The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase:
1.5.1.3;

Protein crystallography data

The structure of The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase, PDB code: 1jom was solved by V.M.Reyes, H.Lee, J.Kraut, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	N/A / 1.90
*Space group*	P 6₅
*Cell size a, b, c (Å), α, β, γ (°)*	96.862, 96.862, 35.022, 90.00, 90.00, 120.00
*R / R_free (%)*	14.2 / n/a

Other elements in 1jom:

The structure of The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase (pdb code 1jom). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase, PDB code: 1jom:

Calcium binding site 1 out of 1 in 1jom

Go back to

Calcium Binding Sites List in 1jom

Calcium binding site 1 out of 1 in the The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase

Mono view

Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Crystal Structure of the Binary Complex Between Folinic Acid (Leucovorin) and E. Coli Dihydrofolate Reductase within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Ca164 b:42.3 occ:1.00	O	A:EOH174	2.3	1.0	1.0
	O	A:MET20	2.6	10.1	1.0
	O	A:GLU17	3.0	23.4	1.0
	O	A:HOH246	3.0	28.7	1.0
	O	A:HOH266	3.1	23.6	1.0
	C	A:ASN18	3.5	18.3	1.0
	N	A:MET20	3.5	19.4	1.0
	O	A:ASN18	3.5	17.7	1.0
	C1	A:EOH174	3.6	46.7	1.0
	O	A:TRP22	3.7	13.6	1.0
	C	A:MET20	3.7	12.6	1.0
	N	A:ALA19	3.8	11.4	1.0
	CA	A:ASN18	3.9	16.9	1.0
	C	A:ALA19	4.0	21.1	1.0
	C	A:GLU17	4.1	23.5	1.0
	CA	A:MET20	4.1	17.5	1.0
	OE2	A:GLU17	4.2	40.0	1.0
	CA	A:ALA19	4.2	17.9	1.0
	N	A:ASN18	4.5	16.2	1.0
	CB	A:MET20	4.8	15.6	1.0
	N	A:PRO21	4.8	15.1	1.0
	O	A:ALA19	4.8	20.1	1.0
	C	A:TRP22	4.9	9.9	1.0
	N	A:TRP22	4.9	11.8	1.0
	C2	A:EOH174	5.0	29.7	1.0
	CD	A:GLU17	5.0	36.9	1.0

Reference:

H.Lee, V.M.Reyes, J.Kraut. Crystal Structures of Escherichia Coli Dihydrofolate Reductase Complexed with 5-Formyltetrahydrofolate (Folinic Acid) in Two Space Groups: Evidence For Enolization of Pteridine O4. Biochemistry V. 35 7012 1996.
ISSN: ISSN 0006-2960
PubMed: 8679526
DOI: 10.1021/BI960028G

Page generated: Thu Jul 11 10:51:48 2024

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