Phosphorus in PDB 1a72: An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad

Enzymatic activity of An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad

All present enzymatic activity of An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad:
1.1.1.1;

Protein crystallography data

The structure of An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad, PDB code: 1a72 was solved by T.D.Colby, B.J.Bahnson, J.K.Chin, J.P.Klinman, B.M.Goldstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.60
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 55.500, 74.200, 179.200, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 30

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad (pdb code 1a72). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad, PDB code: 1a72:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in 1a72

Go back to Phosphorus Binding Sites List in 1a72
Phosphorus binding site 1 out of 2 in the An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P378

b:30.6
occ:1.00
PA A:PAD378 0.0 30.6 1.0
O2A A:PAD378 1.5 32.2 1.0
O1A A:PAD378 1.5 32.4 1.0
O3 A:PAD378 1.6 32.1 1.0
O5B A:PAD378 1.6 32.7 1.0
C5B A:PAD378 2.7 29.6 1.0
PN A:PAD378 3.0 32.1 1.0
O5D A:PAD378 3.0 30.9 1.0
C5D A:PAD378 3.3 29.2 1.0
O2N A:PAD378 3.6 35.5 1.0
O A:HOH435 3.6 42.7 1.0
C4B A:PAD378 3.8 28.0 1.0
C3B A:PAD378 4.0 25.8 1.0
O1N A:PAD378 4.1 33.0 1.0
CA A:GLY201 4.2 16.8 1.0
C4D A:PAD378 4.8 26.8 1.0
N A:GLY201 4.8 18.0 1.0
NH1 A:ARG47 4.9 35.9 1.0
O3B A:PAD378 4.9 25.6 1.0

Phosphorus binding site 2 out of 2 in 1a72

Go back to Phosphorus Binding Sites List in 1a72
Phosphorus binding site 2 out of 2 in the An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of An Active-Site Double Mutant (PHE93->Trp, VAL203->Ala) of Horse Liver Alcohol Dehydrogenase in Complex with the Isosteric Nad Analog Cpad within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P378

b:32.1
occ:1.00
PN A:PAD378 0.0 32.1 1.0
O1N A:PAD378 1.5 33.0 1.0
O2N A:PAD378 1.5 35.5 1.0
O3 A:PAD378 1.6 32.1 1.0
O5D A:PAD378 1.6 30.9 1.0
C5D A:PAD378 2.5 29.2 1.0
PA A:PAD378 3.0 30.6 1.0
O4D A:PAD378 3.3 25.5 1.0
O5B A:PAD378 3.3 32.7 1.0
O1A A:PAD378 3.4 32.4 1.0
C4D A:PAD378 3.4 26.8 1.0
N2N A:PAD378 3.4 34.0 1.0
N7N A:PAD378 3.9 38.1 1.0
CB A:ALA203 3.9 12.3 1.0
CA A:GLY201 4.0 16.8 1.0
C7N A:PAD378 4.0 37.9 1.0
C3N A:PAD378 4.0 35.8 1.0
O A:VAL268 4.1 16.5 1.0
C3D A:PAD378 4.1 27.3 1.0
N A:ALA203 4.2 15.8 1.0
O2A A:PAD378 4.2 32.2 1.0
N A:GLY202 4.2 15.9 1.0
C1N A:PAD378 4.3 31.5 1.0
C5B A:PAD378 4.3 29.6 1.0
C A:GLY201 4.4 16.8 1.0
C1D A:PAD378 4.5 27.7 1.0
N A:GLY201 4.7 18.0 1.0
CA A:ALA203 4.7 14.4 1.0
O7N A:PAD378 4.7 39.5 1.0
O3D A:PAD378 5.0 24.7 1.0

Reference:

T.D.Colby, B.J.Bahnson, J.K.Chin, J.P.Klinman, B.M.Goldstein. Active Site Modifications in A Double Mutant of Liver Alcohol Dehydrogenase: Structural Studies of Two Enzyme-Ligand Complexes. Biochemistry V. 37 9295 1998.
ISSN: ISSN 0006-2960
PubMed: 9649310
DOI: 10.1021/BI973184B
Page generated: Fri Sep 25 12:21:56 2020

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