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Calcium in PDB 1gh4: Structure of the Triple Mutant (K56M, K120M, K121M) of Phospholipase A2

Enzymatic activity of Structure of the Triple Mutant (K56M, K120M, K121M) of Phospholipase A2

All present enzymatic activity of Structure of the Triple Mutant (K56M, K120M, K121M) of Phospholipase A2:
3.1.1.4;

Protein crystallography data

The structure of Structure of the Triple Mutant (K56M, K120M, K121M) of Phospholipase A2, PDB code: 1gh4 was solved by K.Sekar, D.Velmurugan, M.D.Tsai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.20 / 1.90
Space group P 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 39.100, 24.350, 67.110, 90.00, 102.15, 90.00
R / Rfree (%) 19.6 / 25.9

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of the Triple Mutant (K56M, K120M, K121M) of Phospholipase A2 (pdb code 1gh4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of the Triple Mutant (K56M, K120M, K121M) of Phospholipase A2, PDB code: 1gh4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1gh4

Go back to Calcium Binding Sites List in 1gh4
Calcium binding site 1 out of 2 in the Structure of the Triple Mutant (K56M, K120M, K121M) of Phospholipase A2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the Triple Mutant (K56M, K120M, K121M) of Phospholipase A2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca124

b:11.3
occ:1.00
OD2 A:ASP49 2.3 10.1 1.0
O A:GLY30 2.3 15.6 1.0
O A:HOH202 2.4 12.2 1.0
O A:GLY32 2.5 14.4 1.0
O A:TYR28 2.5 8.8 1.0
O A:HOH201 2.7 7.9 1.0
OD1 A:ASP49 2.7 13.4 1.0
CG A:ASP49 2.8 11.1 1.0
C A:GLY32 3.5 14.6 1.0
C A:GLY30 3.5 15.2 1.0
C A:TYR28 3.7 8.9 1.0
N A:GLY32 3.7 14.8 1.0
N A:GLY30 3.8 11.6 1.0
CA A:GLY32 4.1 15.6 1.0
O A:HOH296 4.2 42.5 1.0
C A:LEU31 4.3 17.9 1.0
CB A:ASP49 4.3 10.1 1.0
CA A:GLY30 4.3 14.4 1.0
CA A:TYR28 4.5 9.4 1.0
O A:HOH218 4.5 14.8 1.0
N A:LEU31 4.5 16.6 1.0
CA A:LEU31 4.6 18.0 1.0
N A:GLY33 4.6 15.4 1.0
C A:CYS29 4.6 12.7 1.0
O A:HOH238 4.6 20.4 1.0
N A:CYS29 4.6 8.7 1.0
CA A:CYS29 4.7 9.9 1.0
O A:HOH206 4.7 16.0 1.0
O A:HOH274 4.7 33.4 1.0
O2 A:MPD600 4.8 40.0 1.0
CB A:TYR28 4.8 10.8 1.0
O A:CYS45 4.9 8.0 1.0
CA A:GLY33 4.9 15.6 1.0

Calcium binding site 2 out of 2 in 1gh4

Go back to Calcium Binding Sites List in 1gh4
Calcium binding site 2 out of 2 in the Structure of the Triple Mutant (K56M, K120M, K121M) of Phospholipase A2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of the Triple Mutant (K56M, K120M, K121M) of Phospholipase A2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca125

b:16.9
occ:1.00
O A:HOH241 2.3 14.7 1.0
OE2 A:GLU92 2.3 13.4 1.0
O A:ASN72 2.4 11.5 1.0
O A:HOH235 2.4 15.2 1.0
OD1 A:ASN71 2.5 12.2 1.0
O A:HOH207 2.6 7.8 1.0
CD A:GLU92 3.4 14.8 1.0
C A:ASN72 3.5 8.9 1.0
CG A:ASN71 3.7 14.2 1.0
N A:ASN72 3.7 9.2 1.0
CG A:GLU92 3.8 13.5 1.0
O A:HOH221 4.1 14.1 1.0
CA A:ASN72 4.1 9.3 1.0
C A:ASN71 4.4 8.5 1.0
ND2 A:ASN71 4.4 10.7 1.0
CB A:ASN72 4.5 10.2 1.0
OE1 A:GLU92 4.5 13.0 1.0
O A:HOH258 4.6 42.7 1.0
N A:TYR73 4.7 9.2 1.0
CA A:ASN71 4.7 8.8 1.0
CB A:ASN71 4.8 11.3 1.0
CA A:TYR73 5.0 10.3 1.0

Reference:

V.Rajakannan, M.Yogavel, M.J.Poi, A.A.Jeyaprakash, J.Jeyakanthan, D.Velmurugan, M.D.Tsai, K.Sekar. Observation of Additional Calcium Ion in the Crystal Structure of the Triple Mutant K56,120,121M of Bovine Pancreatic Phospholipase A2. J.Mol.Biol. V. 324 755 2002.
ISSN: ISSN 0022-2836
PubMed: 12460575
DOI: 10.1016/S0022-2836(02)01132-4
Page generated: Sat Dec 12 02:57:45 2020

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