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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy