Fluorine in PDB 3ghs: Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594. Investigation of Global Effects of Radiation Damage on Protein Structure. Second Stage of Radiation Damage.

Enzymatic activity of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594. Investigation of Global Effects of Radiation Damage on Protein Structure. Second Stage of Radiation Damage.

All present enzymatic activity of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594. Investigation of Global Effects of Radiation Damage on Protein Structure. Second Stage of Radiation Damage.:
1.1.1.21;

Protein crystallography data

The structure of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594. Investigation of Global Effects of Radiation Damage on Protein Structure. Second Stage of Radiation Damage., PDB code: 3ghs was solved by T.Petrova, S.Ginell, I.Hazemann, A.Mitschler, A.Podjarny, A.Joachimiak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 1.00
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	49.368, 66.801, 47.355, 90.00, 92.22, 90.00
*R / R_free (%)*	8 / 9.8

Other elements in 3ghs:

Bromine

(Br)

1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594. Investigation of Global Effects of Radiation Damage on Protein Structure. Second Stage of Radiation Damage. (pdb code 3ghs). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594. Investigation of Global Effects of Radiation Damage on Protein Structure. Second Stage of Radiation Damage., PDB code: 3ghs:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 3ghs

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Fluorine Binding Sites List in 3ghs

Fluorine binding site 1 out of 2 in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594. Investigation of Global Effects of Radiation Damage on Protein Structure. Second Stage of Radiation Damage.

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594. Investigation of Global Effects of Radiation Damage on Protein Structure. Second Stage of Radiation Damage. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:F320 b:8.6 occ:1.00	F9	A:LDT320	0.0	8.6	1.0
	C5	A:LDT320	1.3	6.7	1.0
	C2	A:LDT320	2.3	6.7	1.0
	C6	A:LDT320	2.3	7.0	1.0
	O	A:VAL47	3.1	5.0	1.0
	O	A:HOH2029	3.4	10.7	1.0
	O	A:HOH2028	3.6	7.8	1.0
	C3	A:LDT320	3.6	7.3	1.0
	CD1	A:TYR48	3.6	4.5	1.0
	C4	A:LDT320	3.6	6.0	1.0
	C	A:VAL47	3.6	4.3	1.0
	CG1	A:VAL47	3.6	5.1	1.0
	O	A:HOH4002	3.7	11.2	0.5
	O	A:HOH4010	3.7	10.2	0.7
	NE1	A:TRP20	3.8	6.1	1.0
	CG2	A:VAL47	3.9	5.5	1.0
	CD1	A:TRP20	3.9	5.6	1.0
	CA	A:TYR48	3.9	4.7	1.0
	N	A:TYR48	4.0	4.2	1.0
	C7	A:LDT320	4.1	6.7	1.0
	CB	A:VAL47	4.2	4.7	1.0
	CE1	A:TYR48	4.2	4.8	1.0
	CA	A:VAL47	4.5	4.6	1.0
	CG	A:TYR48	4.6	4.4	1.0
	O	A:HOH2189	4.7	10.1	1.0
	O15	A:LDT320	4.8	6.7	1.0
	CB	A:TYR48	4.8	4.6	1.0
	O	A:HOH2017	4.8	8.4	1.0
	CE2	A:TRP20	4.9	6.1	1.0
	C	A:TYR48	4.9	4.6	1.0

Fluorine binding site 2 out of 2 in 3ghs

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Fluorine Binding Sites List in 3ghs

Fluorine binding site 2 out of 2 in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594. Investigation of Global Effects of Radiation Damage on Protein Structure. Second Stage of Radiation Damage.

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594. Investigation of Global Effects of Radiation Damage on Protein Structure. Second Stage of Radiation Damage. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:F320 b:9.8 occ:1.00	F14	A:LDT320	0.0	9.8	1.0
	C27	A:LDT320	1.3	8.0	1.0
	C24	A:LDT320	2.3	7.7	1.0
	C28	A:LDT320	2.4	8.2	1.0
	C13	A:LDT320	2.8	8.3	1.0
	C	A:ALA299	3.0	9.1	1.0
	CA	A:ALA299	3.1	8.8	1.0
	CH2	A:TRP111	3.2	7.0	1.0
	N	A:LEU300	3.3	8.2	1.0
	N	A:ALA299	3.3	8.1	1.0
	O	A:ALA299	3.5	11.1	1.0
	CB	A:LEU300	3.5	8.4	1.0
	C26	A:LDT320	3.6	7.5	1.0
	C25	A:LDT320	3.6	7.9	1.0
	CZ2	A:TRP111	3.7	6.9	1.0
	CZ3	A:TRP111	3.8	6.9	1.0
	C	A:CYS298	3.8	6.0	0.5
	C	A:CYS298	3.8	8.1	0.5
	O	A:CYS298	3.8	6.1	0.5
	CA	A:LEU300	4.0	8.1	1.0
	C29	A:LDT320	4.1	7.4	1.0
	O	A:CYS298	4.1	9.0	0.5
	N17	A:LDT320	4.2	7.8	1.0
	CE2	A:TRP111	4.4	6.0	1.0
	OH	A:TYR309	4.4	10.1	1.0
	CB	A:CYS298	4.5	8.9	0.5
	CE2	A:PHE311	4.5	6.0	0.3
	CA	A:CYS298	4.5	7.8	0.5
	CB	A:ALA299	4.5	11.4	1.0
	CE3	A:TRP111	4.5	6.0	1.0
	SG	A:CYS298	4.5	6.7	0.5
	CE1	A:TYR309	4.7	8.9	1.0
	CA	A:CYS298	4.8	6.1	0.5
	CG	A:LEU300	4.9	9.7	1.0
	CD2	A:TRP111	4.9	5.3	1.0
	CE2	A:PHE311	4.9	6.2	0.5
	CD2	A:LEU300	5.0	11.2	1.0

Reference:

T.Petrova, V.Y.Lunin, S.Ginell, I.Hazemann, K.Lazarski, A.Mitschler, A.Podjarny, A.Joachimiak. X-Ray-Radiation-Induced Cooperative Atomic Movements in Protein. J.Mol.Biol. V. 387 1092 2009.
ISSN: ISSN 0022-2836
PubMed: 19233199
DOI: 10.1016/J.JMB.2009.02.030

Page generated: Wed Jul 31 18:53:20 2024

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