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Manganese in PDB 1sfy: Crystal Structure of Recombinant Erythrina Corallodandron Lectin

Protein crystallography data

The structure of Crystal Structure of Recombinant Erythrina Corallodandron Lectin, PDB code: 1sfy was solved by K.A.Kulkarni, A.Srivastava, N.Mitra, A.Surolia, M.Vijayan, K.Suguna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.66 / 2.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 87.240, 144.890, 127.660, 90.00, 93.29, 90.00
R / Rfree (%) 18 / 20.8

Other elements in 1sfy:

The structure of Crystal Structure of Recombinant Erythrina Corallodandron Lectin also contains other interesting chemical elements:

Calcium (Ca) 6 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Recombinant Erythrina Corallodandron Lectin (pdb code 1sfy). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the Crystal Structure of Recombinant Erythrina Corallodandron Lectin, PDB code: 1sfy:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in 1sfy

Go back to Manganese Binding Sites List in 1sfy
Manganese binding site 1 out of 6 in the Crystal Structure of Recombinant Erythrina Corallodandron Lectin


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 Recombinant Erythrina Corallodandron Lectin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1289

b:22.8
occ:1.00
OD1 A:ASP136 1.9 39.8 1.0
O A:HOH1501 2.1 26.0 1.0
OE2 A:GLU127 2.2 21.7 1.0
NE2 A:HIS142 2.3 21.3 1.0
OD2 A:ASP129 2.3 29.4 1.0
O A:HOH1500 2.3 21.6 1.0
CG A:ASP136 3.0 37.7 1.0
CE1 A:HIS142 3.1 21.6 1.0
CG A:ASP129 3.2 27.6 1.0
CD A:GLU127 3.2 22.2 1.0
CD2 A:HIS142 3.4 23.2 1.0
CB A:ASP129 3.5 26.0 1.0
OE1 A:GLU127 3.6 24.0 1.0
OD2 A:ASP136 3.6 36.6 1.0
CB A:ASP136 4.2 38.0 1.0
OG A:SER152 4.2 30.6 1.0
ND1 A:HIS142 4.3 24.7 1.0
OD1 A:ASP129 4.4 28.6 1.0
O A:HOH1638 4.4 26.6 1.0
O A:HOH1502 4.5 15.8 1.0
CA A:CA1290 4.5 36.9 1.0
CG A:HIS142 4.5 24.3 1.0
O A:ILE150 4.6 30.2 1.0
CG A:GLU127 4.6 21.4 1.0
NE1 A:TRP135 4.8 37.4 1.0
CA A:ASP136 4.8 38.6 1.0
CD A:PRO137 4.8 38.8 1.0
CD1 A:TRP135 4.9 37.5 1.0

Manganese binding site 2 out of 6 in 1sfy

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Manganese binding site 2 out of 6 in the Crystal Structure of Recombinant Erythrina Corallodandron Lectin


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 Recombinant Erythrina Corallodandron Lectin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn2289

b:25.6
occ:1.00
OD1 B:ASP136 2.1 39.9 1.0
O B:HOH2500 2.2 18.7 1.0
OE2 B:GLU127 2.3 19.5 1.0
OD2 B:ASP129 2.3 27.4 1.0
O B:HOH2501 2.3 31.0 1.0
NE2 B:HIS142 2.3 24.5 1.0
CE1 B:HIS142 3.1 24.7 1.0
CG B:ASP136 3.1 37.7 1.0
CG B:ASP129 3.2 27.3 1.0
CD B:GLU127 3.3 19.6 1.0
CD2 B:HIS142 3.5 25.5 1.0
CB B:ASP129 3.5 26.7 1.0
OE1 B:GLU127 3.6 19.7 1.0
OD2 B:ASP136 3.7 35.7 1.0
O B:HOH2502 4.1 25.6 1.0
CB B:ASP136 4.1 37.0 1.0
OG B:SER152 4.2 32.0 1.0
ND1 B:HIS142 4.3 25.9 1.0
CA B:CA2290 4.3 29.4 1.0
OD1 B:ASP129 4.3 28.9 1.0
O B:HOH2572 4.5 21.0 1.0
CG B:HIS142 4.5 24.9 1.0
O B:ILE150 4.5 32.1 1.0
CG B:GLU127 4.6 20.4 1.0
NE1 B:TRP135 4.7 38.3 1.0
CA B:ASP136 4.8 38.3 1.0
CD B:PRO137 4.8 39.9 1.0
CD1 B:TRP135 4.9 38.0 1.0

Manganese binding site 3 out of 6 in 1sfy

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Manganese binding site 3 out of 6 in the Crystal Structure of Recombinant Erythrina Corallodandron Lectin


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 Recombinant Erythrina Corallodandron Lectin within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn3289

b:19.7
occ:1.00
OD1 C:ASP136 2.2 36.8 1.0
OE2 C:GLU127 2.2 19.2 1.0
O C:HOH3501 2.2 21.2 1.0
O C:HOH3500 2.2 6.3 1.0
OD2 C:ASP129 2.3 25.2 1.0
NE2 C:HIS142 2.3 21.1 1.0
CE1 C:HIS142 3.1 18.9 1.0
CG C:ASP136 3.1 37.4 1.0
CG C:ASP129 3.2 26.3 1.0
CD C:GLU127 3.2 20.2 1.0
CD2 C:HIS142 3.5 22.5 1.0
CB C:ASP129 3.5 25.9 1.0
OE1 C:GLU127 3.5 19.7 1.0
OD2 C:ASP136 3.7 36.3 1.0
O C:HOH3502 3.9 18.6 1.0
O C:HOH3608 4.2 28.7 1.0
CB C:ASP136 4.2 38.1 1.0
OG C:SER152 4.2 26.9 1.0
ND1 C:HIS142 4.3 20.9 1.0
OD1 C:ASP129 4.3 28.3 1.0
CA C:CA3290 4.4 27.3 1.0
CG C:HIS142 4.5 22.7 1.0
O C:ILE150 4.6 29.8 1.0
CG C:GLU127 4.6 21.2 1.0
NE1 C:TRP135 4.8 36.3 1.0
CA C:ASP136 4.8 38.5 1.0
CD C:PRO137 4.9 38.1 1.0
CD1 C:TRP135 4.9 36.5 1.0
CA C:ASP129 5.0 25.4 1.0

Manganese binding site 4 out of 6 in 1sfy

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Manganese binding site 4 out of 6 in the Crystal Structure of Recombinant Erythrina Corallodandron Lectin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Recombinant Erythrina Corallodandron Lectin within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn4289

b:22.2
occ:1.00
OE2 D:GLU127 2.2 22.6 1.0
NE2 D:HIS142 2.2 24.3 1.0
OD1 D:ASP136 2.3 38.6 1.0
O D:HOH4500 2.3 10.2 1.0
OD2 D:ASP129 2.3 26.6 1.0
O D:HOH4501 2.3 29.6 1.0
CE1 D:HIS142 3.0 24.4 1.0
CG D:ASP129 3.2 27.7 1.0
CD D:GLU127 3.3 22.6 1.0
CG D:ASP136 3.3 38.5 1.0
CD2 D:HIS142 3.4 24.4 1.0
CB D:ASP129 3.5 26.2 1.0
OE1 D:GLU127 3.6 22.7 1.0
OD2 D:ASP136 4.0 37.5 1.0
O D:HOH4502 4.1 13.5 1.0
CB D:ASP136 4.2 38.3 1.0
ND1 D:HIS142 4.2 25.5 1.0
OG D:SER152 4.2 28.6 1.0
OD1 D:ASP129 4.3 29.6 1.0
CG D:HIS142 4.4 25.1 1.0
CA D:CA4290 4.4 31.9 1.0
CG D:GLU127 4.6 20.7 1.0
O D:ILE150 4.6 32.8 1.0
CD D:PRO137 4.8 38.7 1.0
CA D:ASP136 4.8 39.0 1.0
NE1 D:TRP135 4.9 35.8 1.0
CA D:ASP129 5.0 25.6 1.0
CD1 D:TRP135 5.0 36.8 1.0

Manganese binding site 5 out of 6 in 1sfy

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Manganese binding site 5 out of 6 in the Crystal Structure of Recombinant Erythrina Corallodandron Lectin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of Recombinant Erythrina Corallodandron Lectin within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn5289

b:27.6
occ:1.00
OD1 E:ASP136 2.1 38.7 1.0
O E:HOH5501 2.2 24.4 1.0
OE2 E:GLU127 2.3 22.3 1.0
NE2 E:HIS142 2.3 24.5 1.0
O E:HOH5500 2.3 19.5 1.0
OD2 E:ASP129 2.4 29.2 1.0
CE1 E:HIS142 3.1 25.1 1.0
CG E:ASP136 3.1 38.6 1.0
CD E:GLU127 3.3 22.8 1.0
CG E:ASP129 3.3 29.0 1.0
CD2 E:HIS142 3.4 24.4 1.0
CB E:ASP129 3.6 27.3 1.0
OE1 E:GLU127 3.6 24.3 1.0
OD2 E:ASP136 3.7 38.1 1.0
OG E:SER152 4.1 27.7 1.0
CB E:ASP136 4.1 38.5 1.0
O E:HOH5502 4.2 20.1 1.0
ND1 E:HIS142 4.3 27.1 1.0
OD1 E:ASP129 4.4 29.2 1.0
CG E:HIS142 4.5 26.2 1.0
O E:ILE150 4.5 32.9 1.0
CA E:CA5290 4.6 37.5 1.0
CG E:GLU127 4.6 22.4 1.0
CD E:PRO137 4.7 40.7 1.0
CA E:ASP136 4.8 39.2 1.0
NE1 E:TRP135 4.8 37.4 1.0
CD1 E:TRP135 4.9 38.4 1.0

Manganese binding site 6 out of 6 in 1sfy

Go back to Manganese Binding Sites List in 1sfy
Manganese binding site 6 out of 6 in the Crystal Structure of Recombinant Erythrina Corallodandron Lectin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of Recombinant Erythrina Corallodandron Lectin within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mn6289

b:25.4
occ:1.00
O F:HOH6501 2.1 20.9 1.0
OD1 F:ASP136 2.2 37.6 1.0
OD2 F:ASP129 2.2 25.9 1.0
NE2 F:HIS142 2.2 23.7 1.0
OE2 F:GLU127 2.3 21.8 1.0
O F:HOH6500 2.3 10.6 1.0
CE1 F:HIS142 3.0 22.9 1.0
CG F:ASP136 3.1 38.8 1.0
CG F:ASP129 3.1 28.8 1.0
CD F:GLU127 3.3 22.7 1.0
CD2 F:HIS142 3.4 24.6 1.0
CB F:ASP129 3.4 27.3 1.0
OD2 F:ASP136 3.6 39.2 1.0
OE1 F:GLU127 3.7 22.2 1.0
O F:HOH6502 3.9 21.8 1.0
CB F:ASP136 4.1 39.4 1.0
ND1 F:HIS142 4.2 24.2 1.0
OD1 F:ASP129 4.2 32.6 1.0
CA F:CA6290 4.3 33.4 1.0
OG F:SER152 4.4 31.3 1.0
CG F:HIS142 4.4 24.4 1.0
CG F:GLU127 4.6 22.7 1.0
O F:ILE150 4.7 32.6 1.0
CA F:ASP136 4.8 39.8 1.0
CD F:PRO137 4.8 40.4 1.0
NE1 F:TRP135 4.8 38.2 1.0
CA F:ASP129 4.9 26.4 1.0
CD1 F:TRP135 5.0 37.6 1.0

Reference:

K.A.Kulkarni, A.Srivastava, N.Mitra, N.Sharon, A.Surolia, M.Vijayan, K.Suguna. Effect of Glycosylation on the Structure of Erythrina Corallodendron Lectin. Proteins V. 56 821 2004.
ISSN: ISSN 0887-3585
PubMed: 15281133
DOI: 10.1002/PROT.20168
Page generated: Tue Dec 15 03:55:34 2020

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