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Manganese in PDB 1m4z: Crystal Structure of the N-Terminal Bah Domain of ORC1P

Protein crystallography data

The structure of Crystal Structure of the N-Terminal Bah Domain of ORC1P, PDB code: 1m4z was solved by Z.Zhang, M.K.Hayashi, O.Merkel, B.Stillman, R.-M.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.20
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 128.260, 61.050, 67.770, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 22.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the N-Terminal Bah Domain of ORC1P (pdb code 1m4z). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Crystal Structure of the N-Terminal Bah Domain of ORC1P, PDB code: 1m4z:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 1m4z

Go back to Manganese Binding Sites List in 1m4z
Manganese binding site 1 out of 3 in the Crystal Structure of the N-Terminal Bah Domain of ORC1P


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the N-Terminal Bah Domain of ORC1P within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:23.3
occ:0.50
OE2 A:GLU61 2.3 27.6 1.0
OE2 B:GLU61 2.4 23.5 1.0
OE1 B:GLU61 2.6 23.7 1.0
OE1 A:GLU61 2.7 27.9 1.0
CD A:GLU61 2.8 27.4 1.0
CD B:GLU61 2.8 22.4 1.0
O B:HOH534 3.5 36.0 1.0
O B:HOH535 3.7 31.9 1.0
O B:HOH528 4.2 19.2 1.0
O A:HOH548 4.3 20.6 1.0
CG A:GLU61 4.3 23.2 1.0
CG B:GLU61 4.3 22.0 1.0
O B:HOH554 4.9 33.8 1.0

Manganese binding site 2 out of 3 in 1m4z

Go back to Manganese Binding Sites List in 1m4z
Manganese binding site 2 out of 3 in the Crystal Structure of the N-Terminal Bah Domain of ORC1P


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the N-Terminal Bah Domain of ORC1P within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn503

b:47.8
occ:1.00
O B:HOH540 2.1 17.6 1.0
O B:HOH541 2.1 21.5 1.0
O A:HOH544 2.2 19.0 1.0
O B:HOH543 2.2 23.5 1.0
O B:HOH542 2.3 25.4 1.0
OE2 A:GLU84 2.3 29.8 1.0
CD A:GLU84 3.1 27.8 1.0
OE1 A:GLU84 3.2 27.0 1.0
O A:HOH559 4.0 28.4 1.0
OE1 B:GLU137 4.0 19.4 1.0
O B:HOH512 4.1 24.4 1.0
OE2 B:GLU95 4.1 30.8 1.0
O B:HOH615 4.1 44.3 1.0
O B:HOH520 4.2 24.9 1.0
O B:HOH511 4.3 19.4 1.0
O B:HOH504 4.5 16.4 1.0
CG A:GLU84 4.5 28.3 1.0
OE2 A:GLU140 4.5 21.9 1.0
O B:PRO179 4.6 25.7 1.0
CD2 B:LEU91 4.7 19.0 1.0
OE1 A:GLU140 4.9 26.3 1.0

Manganese binding site 3 out of 3 in 1m4z

Go back to Manganese Binding Sites List in 1m4z
Manganese binding site 3 out of 3 in the Crystal Structure of the N-Terminal Bah Domain of ORC1P


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of the N-Terminal Bah Domain of ORC1P within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:49.4
occ:1.00
OE2 B:GLU84 2.1 25.1 1.0
O A:HOH545 2.2 21.0 1.0
O B:HOH545 2.2 29.1 1.0
O A:HOH546 2.2 22.4 1.0
O A:HOH547 2.2 23.0 1.0
O B:HOH544 2.2 17.1 1.0
CD B:GLU84 3.1 21.6 1.0
OE1 B:GLU84 3.3 19.9 1.0
OE1 A:GLU137 4.0 19.6 1.0
O A:HOH515 4.0 15.8 1.0
O B:HOH574 4.0 34.2 1.0
O B:HOH578 4.1 39.4 1.0
O A:HOH510 4.1 13.4 1.0
OE2 A:GLU95 4.2 23.6 1.0
O B:HOH507 4.2 21.8 1.0
CG B:GLU84 4.4 22.8 1.0
O A:HOH509 4.4 20.5 1.0
OE2 B:GLU140 4.5 23.8 1.0
CD2 A:LEU91 4.7 13.5 1.0
O A:PRO179 4.7 24.8 1.0
O A:HOH622 4.9 33.2 1.0

Reference:

Z.Zhang, M.K.Hayashi, O.Merkel, B.Stillman, R.M.Xu. Structure and Function of the Bah-Containing Domain of ORC1P in Epigenetic Silencing. Embo J. V. 21 4600 2002.
ISSN: ISSN 0261-4189
PubMed: 12198162
DOI: 10.1093/EMBOJ/CDF468
Page generated: Sat Oct 5 11:38:39 2024

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