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Manganese in PDB 1rqq: Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of Aps

Enzymatic activity of Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of Aps

All present enzymatic activity of Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of Aps:
2.7.1.112;

Protein crystallography data

The structure of Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of Aps, PDB code: 1rqq was solved by J.Hu, J.Liu, R.Ghirlando, A.R.Saltiel, S.R.Hubbard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 87.216, 96.443, 121.993, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 27.7

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of Aps (pdb code 1rqq). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of Aps, PDB code: 1rqq:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1rqq

Go back to Manganese Binding Sites List in 1rqq
Manganese binding site 1 out of 2 in the Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of Aps


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 Insulin Receptor Kinase in Complex with the SH2 Domain of Aps within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:35.4
occ:1.00
O A:HOH63 1.9 22.2 1.0
O2S E:112117 2.1 48.9 1.0
OD2 A:ASP1150 2.1 36.9 1.0
O2G E:112117 2.2 48.4 1.0
O2B E:112117 2.2 40.0 1.0
OD1 A:ASN1137 2.2 30.7 1.0
C2S E:112117 3.0 48.1 1.0
PG E:112117 3.2 49.6 1.0
C1S E:112117 3.2 49.1 1.0
CG A:ASP1150 3.2 35.7 1.0
CG A:ASN1137 3.3 31.6 1.0
PB E:112117 3.3 41.9 1.0
O3B E:112117 3.4 45.6 1.0
ND2 A:ASN1137 3.7 30.7 1.0
CB A:ASP1150 3.8 31.9 1.0
S1G E:112117 3.9 54.0 1.0
O2A E:112117 4.0 42.6 1.0
O E:HOH62 4.1 38.0 1.0
O3A E:112117 4.2 42.8 1.0
O E:HOH64 4.2 49.0 1.0
O A:HOH1 4.2 34.9 1.0
NS E:112117 4.2 44.9 1.0
OD1 A:ASP1150 4.3 36.1 1.0
O1B E:112117 4.5 42.5 1.0
CB A:ASN1137 4.5 32.8 1.0
O3G E:112117 4.6 48.7 1.0
NE A:ARG1136 4.6 43.4 1.0
CD A:ARG1136 4.6 39.8 1.0
O A:ARG1136 4.7 35.2 1.0
PA E:112117 4.7 40.7 1.0
CA A:ASN1137 4.8 34.1 1.0
CG A:ARG1136 4.9 37.6 1.0
OD2 A:ASP1132 4.9 30.7 1.0
O A:HOH22 4.9 41.1 1.0
C A:ARG1136 5.0 35.1 1.0

Manganese binding site 2 out of 2 in 1rqq

Go back to Manganese Binding Sites List in 1rqq
Manganese binding site 2 out of 2 in the Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of Aps


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 Insulin Receptor Kinase in Complex with the SH2 Domain of Aps within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn202

b:35.5
occ:1.00
OD2 B:ASP1150 2.0 33.5 1.0
O2G F:112117 2.1 53.8 1.0
O2B F:112117 2.2 46.6 1.0
OD1 B:ASN1137 2.2 35.3 1.0
O F:HOH66 2.2 17.6 1.0
O2S F:112117 2.3 48.7 1.0
C2S F:112117 3.1 50.9 1.0
PG F:112117 3.1 52.5 1.0
CG B:ASP1150 3.1 34.1 1.0
C1S F:112117 3.2 54.2 1.0
CG B:ASN1137 3.2 33.1 1.0
PB F:112117 3.3 42.2 1.0
O3B F:112117 3.4 48.6 1.0
ND2 B:ASN1137 3.7 30.5 1.0
S1G F:112117 3.7 62.2 1.0
CB B:ASP1150 3.7 30.9 1.0
O3A F:112117 4.1 48.3 1.0
O2A F:112117 4.2 51.7 1.0
OD1 B:ASP1150 4.2 31.5 1.0
NS F:112117 4.3 48.7 1.0
O F:HOH11 4.3 42.7 1.0
O1B F:112117 4.4 47.5 1.0
O3G F:112117 4.4 53.8 1.0
CB B:ASN1137 4.5 33.0 1.0
O B:ARG1136 4.7 36.0 1.0
CA B:ASN1137 4.8 34.9 1.0
PA F:112117 4.8 48.4 1.0
O B:HOH67 4.8 43.2 1.0
OD1 B:ASP1132 5.0 26.6 1.0
C B:ARG1136 5.0 35.6 1.0

Reference:

J.Hu, J.Liu, R.Ghirlando, A.R.Saltiel, S.R.Hubbard. Structural Basis For Recruitment of the Adaptor Protein Aps to the Activated Insulin Receptor. Mol.Cell V. 12 1379 2003.
ISSN: ISSN 1097-2765
PubMed: 14690593
DOI: 10.1016/S1097-2765(03)00487-8
Page generated: Sat Oct 5 12:20:48 2024

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