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Manganese in PDB 1it6: Crystal Structure of the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1

Enzymatic activity of Crystal Structure of the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1

All present enzymatic activity of Crystal Structure of the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1:
3.1.3.16;

Protein crystallography data

The structure of Crystal Structure of the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1, PDB code: 1it6 was solved by A.Kita, S.Matsunaga, A.Takai, H.Kataiwa, T.Wakimoto, N.Fusetani, M.Isobe, K.Miki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 98.090, 136.360, 61.580, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 21.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1 (pdb code 1it6). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1, PDB code: 1it6:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1it6

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Manganese binding site 1 out of 4 in the Crystal Structure of the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1


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 Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:12.1
occ:1.00
 O A:HOH602 2.3 13.7 1.0
NE2 A:HIS66 2.3 6.7 1.0
O A:HOH601 2.3 13.6 1.0
OD1 A:ASP64 2.4 12.1 1.0
OD2 A:ASP92 2.4 13.5 1.0
MN A:MN402 3.3 14.6 1.0
CD2 A:HIS66 3.3 6.0 1.0
CE1 A:HIS66 3.3 7.0 1.0
CG A:ASP64 3.3 11.2 1.0
CG A:ASP92 3.4 11.7 1.0
O A:HIS248 3.8 14.2 1.0
CB A:ASP92 3.8 9.9 1.0
CB A:ASP64 4.0 9.8 1.0
O A:HOH612 4.1 5.7 1.0
O6 A:CYU501 4.2 12.4 1.0
OD2 A:ASP64 4.2 12.2 1.0
CD2 A:HIS125 4.3 7.9 1.0
CE1 A:PHE267 4.3 8.9 1.0
OH A:TYR272 4.4 10.2 1.0
ND1 A:HIS66 4.4 6.1 1.0
C A:HIS248 4.4 13.4 1.0
CG A:HIS66 4.5 6.0 1.0
CA A:HIS248 4.5 10.6 1.0
NE2 A:HIS125 4.5 5.9 1.0
OD1 A:ASP92 4.5 12.6 1.0
NE2 A:HIS173 4.6 5.4 1.0
OD1 A:ASN124 4.7 14.6 1.0
CZ A:PHE267 4.8 8.8 1.0
CE1 A:HIS173 4.8 6.8 1.0
ND1 A:HIS248 5.0 7.4 1.0

Manganese binding site 2 out of 4 in 1it6

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Manganese binding site 2 out of 4 in the Crystal Structure of the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1


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 Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn402

b:14.6
occ:1.00
 OD1 A:ASN124 2.3 14.6 1.0
O A:HOH601 2.3 13.6 1.0
NE2 A:HIS173 2.3 5.4 1.0
ND1 A:HIS248 2.4 7.4 1.0
OD2 A:ASP92 2.5 13.5 1.0
CG A:ASN124 3.2 13.1 1.0
CD2 A:HIS173 3.2 5.0 1.0
CE1 A:HIS248 3.3 6.5 1.0
MN A:MN401 3.3 12.1 1.0
CE1 A:HIS173 3.4 6.8 1.0
CG A:ASP92 3.4 11.7 1.0
CG A:HIS248 3.4 8.1 1.0
CA A:HIS248 3.6 10.6 1.0
O A:HOH612 3.6 5.7 1.0
OD1 A:ASP92 3.7 12.6 1.0
CB A:HIS248 3.8 8.9 1.0
ND2 A:ASN124 3.8 11.6 1.0
O A:HIS248 3.9 14.2 1.0
CD2 A:HIS125 4.2 7.9 1.0
OD1 A:ASP64 4.2 12.1 1.0
C A:HIS248 4.2 13.4 1.0
CB A:ASN124 4.3 9.5 1.0
N A:ASN124 4.3 9.6 1.0
CG A:HIS173 4.4 5.0 1.0
NE2 A:HIS248 4.5 9.1 1.0
ND1 A:HIS173 4.5 7.0 1.0
N A:HIS248 4.5 11.6 1.0
CD2 A:HIS248 4.6 7.6 1.0
O A:LEU205 4.6 12.3 1.0
CB A:ASP92 4.6 9.9 1.0
NE2 A:HIS125 4.8 5.9 1.0
CA A:ASN124 4.9 10.4 1.0
O A:HOH602 4.9 13.7 1.0
CG A:ASP64 4.9 11.2 1.0
OD2 A:ASP64 5.0 12.2 1.0

Manganese binding site 3 out of 4 in 1it6

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Manganese binding site 3 out of 4 in the Crystal Structure of the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1


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 Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn401

b:15.2
occ:1.00
 O B:HOH604 2.3 14.4 1.0
O B:HOH603 2.3 13.5 1.0
OD2 B:ASP64 2.4 13.0 1.0
NE2 B:HIS66 2.4 11.2 1.0
OD2 B:ASP92 2.4 11.7 1.0
MN B:MN402 3.1 15.8 1.0
CD2 B:HIS66 3.3 10.9 1.0
CG B:ASP64 3.4 15.6 1.0
CE1 B:HIS66 3.4 11.8 1.0
CG B:ASP92 3.5 14.4 1.0
O B:HIS248 3.8 12.5 1.0
O B:HOH615 3.8 16.8 1.0
CB B:ASP92 4.0 11.2 1.0
O6 B:CYU1501 4.0 14.4 1.0
CB B:ASP64 4.1 14.0 1.0
OD1 B:ASP64 4.3 13.9 1.0
CD2 B:HIS125 4.3 11.3 1.0
CA B:HIS248 4.4 11.6 1.0
CE1 B:PHE267 4.4 19.3 1.0
C B:HIS248 4.4 13.8 1.0
OH B:TYR272 4.4 17.4 1.0
CG B:HIS66 4.5 10.9 1.0
NE2 B:HIS125 4.5 10.4 1.0
NE2 B:HIS173 4.5 8.4 1.0
ND1 B:HIS66 4.5 11.4 1.0
OD1 B:ASP92 4.6 15.4 1.0
OD1 B:ASN124 4.7 13.2 1.0
ND1 B:HIS248 4.8 7.5 1.0
CE1 B:HIS173 4.8 9.7 1.0

Manganese binding site 4 out of 4 in 1it6

Go back to Manganese Binding Sites List in 1it6
Manganese binding site 4 out of 4 in the Crystal Structure of the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1


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 the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn402

b:15.8
occ:1.00
 OD1 B:ASN124 2.3 13.2 1.0
O B:HOH603 2.3 13.5 1.0
NE2 B:HIS173 2.3 8.4 1.0
ND1 B:HIS248 2.4 7.5 1.0
OD2 B:ASP92 2.4 11.7 1.0
MN B:MN401 3.1 15.2 1.0
CG B:ASN124 3.2 11.5 1.0
CD2 B:HIS173 3.3 7.2 1.0
CE1 B:HIS248 3.3 6.2 1.0
CG B:ASP92 3.3 14.4 1.0
CE1 B:HIS173 3.4 9.7 1.0
CG B:HIS248 3.4 8.5 1.0
O B:HOH615 3.5 16.8 1.0
CA B:HIS248 3.5 11.6 1.0
OD1 B:ASP92 3.7 15.4 1.0
ND2 B:ASN124 3.7 9.4 1.0
CB B:HIS248 3.7 9.1 1.0
O B:HIS248 3.9 12.5 1.0
OD2 B:ASP64 4.1 13.0 1.0
CD2 B:HIS125 4.2 11.3 1.0
C B:HIS248 4.2 13.8 1.0
N B:ASN124 4.4 9.6 1.0
CB B:ASN124 4.5 9.9 1.0
CG B:HIS173 4.5 9.6 1.0
NE2 B:HIS248 4.5 8.8 1.0
ND1 B:HIS173 4.5 10.0 1.0
N B:HIS248 4.5 11.8 1.0
CD2 B:HIS248 4.5 7.7 1.0
CB B:ASP92 4.6 11.2 1.0
O B:LEU205 4.7 12.6 1.0
CG B:ASP64 4.8 15.6 1.0
O B:HOH604 4.8 14.4 1.0
NE2 B:HIS125 4.9 10.4 1.0
NE2 B:HIS66 4.9 11.2 1.0
OD1 B:ASP64 4.9 13.9 1.0
CA B:ASN124 5.0 10.3 1.0

Reference:

A.Kita, S.Matsunaga, A.Takai, H.Kataiwa, T.Wakimoto, N.Fusetani, M.Isobe, K.Miki. Crystal Structure of the Complex Between Calyculin A and the Catalytic Subunit of Protein Phosphatase 1. Structure V. 10 715 2002.
ISSN: ISSN 0969-2126
PubMed: 12015153
DOI: 10.1016/S0969-2126(02)00764-5
Page generated: Sat Oct 5 11:03:46 2024

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