Atomistry » Manganese » PDB 1ho5-1j53 » 1it6
Atomistry »
  Manganese »
    PDB 1ho5-1j53 »
      1it6 »

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

Go back to Manganese Binding Sites List in 1it6
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

Go back to Manganese Binding Sites List in 1it6
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

Go back to Manganese Binding Sites List in 1it6
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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy