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Calcium in PDB 2p69: Crystal Structure of Human Pyridoxal Phosphate Phosphatase with Plp

Enzymatic activity of Crystal Structure of Human Pyridoxal Phosphate Phosphatase with Plp

All present enzymatic activity of Crystal Structure of Human Pyridoxal Phosphate Phosphatase with Plp:
3.1.3.74;

Protein crystallography data

The structure of Crystal Structure of Human Pyridoxal Phosphate Phosphatase with Plp, PDB code: 2p69 was solved by U.A.Ramagopal, J.Freeman, M.Izuka, R.Toro, J.M.Sauder, S.K.Burley, S.C.Almo, New York Sgx Research Center For Structural Genomics(Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.27 / 2.25
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 54.559, 54.559, 212.537, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 25

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Human Pyridoxal Phosphate Phosphatase with Plp (pdb code 2p69). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Human Pyridoxal Phosphate Phosphatase with Plp, PDB code: 2p69:

Calcium binding site 1 out of 1 in 2p69

Go back to Calcium Binding Sites List in 2p69
Calcium binding site 1 out of 1 in the Crystal Structure of Human Pyridoxal Phosphate Phosphatase with Plp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Human Pyridoxal Phosphate Phosphatase with Plp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca305

b:42.1
occ:1.00
O3P A:PLP306 2.2 39.8 1.0
O A:HOH335 2.3 37.5 1.0
OD2 A:ASP25 2.4 42.2 1.0
O A:HOH343 2.4 33.4 1.0
OD1 A:ASP238 2.4 41.9 1.0
O A:ASP27 2.5 42.4 1.0
OD1 A:ASP25 2.7 41.2 1.0
CG A:ASP25 2.9 44.1 1.0
CG A:ASP238 3.4 38.1 1.0
P A:PLP306 3.5 43.8 1.0
C A:ASP27 3.6 37.3 1.0
O A:HOH336 3.7 49.8 1.0
OD2 A:ASP238 3.8 36.3 1.0
O2P A:PLP306 3.9 40.4 1.0
OD2 A:ASP243 4.0 38.8 1.0
N A:ASP27 4.1 40.3 1.0
O A:HOH326 4.1 46.1 1.0
O1P A:PLP306 4.1 42.1 1.0
CA A:ASP27 4.2 39.8 1.0
CB A:ASP27 4.4 39.5 1.0
CB A:ASP25 4.4 39.6 1.0
OD1 A:ASP243 4.6 36.4 1.0
CB A:ASP238 4.7 32.9 1.0
N A:CYS26 4.7 39.2 1.0
CG2 A:VAL29 4.7 33.2 1.0
O4P A:PLP306 4.7 48.6 1.0
N A:GLY28 4.7 41.2 1.0
CG A:ASP243 4.7 43.3 1.0
NZ A:LYS213 4.7 36.2 1.0
OD2 A:ASP27 4.8 62.7 1.0
N A:ASP238 4.8 38.9 1.0
C A:CYS26 4.8 43.2 1.0
C5A A:PLP306 4.9 51.7 1.0

Reference:

S.C.Almo, J.B.Bonanno, J.M.Sauder, S.Emtage, T.P.Dilorenzo, V.Malashkevich, S.R.Wasserman, S.Swaminathan, S.Eswaramoorthy, R.Agarwal, D.Kumaran, M.Madegowda, S.Ragumani, Y.Patskovsky, J.Alvarado, U.A.Ramagopal, J.Faber-Barata, M.R.Chance, A.Sali, A.Fiser, Z.Y.Zhang, D.S.Lawrence, S.K.Burley. Structural Genomics of Protein Phosphatases. J.Struct.Funct.Genom. V. 8 121 2007.
ISSN: ISSN 1345-711X
PubMed: 18058037
DOI: 10.1007/S10969-007-9036-1
Page generated: Fri Jul 12 15:00:45 2024

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