Chlorine in PDB 2toh: Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat

Enzymatic activity of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat

All present enzymatic activity of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat:
1.14.16.2;

Protein crystallography data

The structure of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat, PDB code: 2toh was solved by K.E.Goodwill, C.Sabatier, R.C.Stevens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	40.00 / 2.30
*Space group*	F 2 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	189.464, 148.595, 56.986, 90.00, 90.00, 90.00
*R / R_free (%)*	20.7 / 27.6

Other elements in 2toh:

The structure of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat also contains other interesting chemical elements:

Iron

(Fe)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat (pdb code 2toh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat, PDB code: 2toh:

Chlorine binding site 1 out of 1 in 2toh

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Chlorine Binding Sites List in 2toh

Chlorine binding site 1 out of 1 in the Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl510 b:55.5 occ:1.00	ND2	A:ASN439	3.5	59.8	1.0
	O	A:HOH617	3.7	30.7	1.0
	N	A:PHE438	3.7	39.5	1.0
	N	A:ASN439	3.9	43.1	1.0
	CB	A:SER437	4.0	39.8	1.0
	CG	A:ASN439	4.3	58.6	1.0
	OG	A:SER437	4.3	36.2	1.0
	O	A:HOH666	4.4	67.0	1.0
	O	A:HOH626	4.4	72.3	1.0
	CA	A:PHE438	4.5	37.8	1.0
	CB	A:PHE438	4.5	38.2	1.0
	C	A:SER437	4.5	41.4	1.0
	CB	A:ASN439	4.5	51.4	1.0
	CA	A:SER437	4.6	38.5	1.0
	OE2	A:GLU251	4.7	37.4	1.0
	C	A:PHE438	4.7	38.8	1.0
	CD1	A:PHE438	4.8	35.3	1.0
	CA	A:ASN439	4.8	47.5	1.0
	OG1	A:THR344	4.8	31.1	1.0
	CG2	A:THR344	4.9	28.5	1.0
	O	A:HOH665	5.0	48.7	1.0
	NH2	A:ARG250	5.0	68.9	1.0

Reference:

K.E.Goodwill, C.Sabatier, R.C.Stevens. Crystal Structure of Tyrosine Hydroxylase with Bound Cofactor Analogue and Iron at 2.3 A Resolution: Self-Hydroxylation of PHE300 and the Pterin-Binding Site. Biochemistry V. 37 13437 1998.
ISSN: ISSN 0006-2960
PubMed: 9753429
DOI: 10.1021/BI981462G

Page generated: Sat Jul 20 11:23:15 2024

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