Copper in PDB 6an3: Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound)

Enzymatic activity of Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound)

All present enzymatic activity of Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound):
1.14.17.3; 4.3.2.5;

Protein crystallography data

The structure of Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound), PDB code: 6an3 was solved by S.Maheshwari, K.Rudzka, S.B.Gabelli, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	48.43 / 2.05
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	59.029, 66.847, 70.246, 90.00, 90.00, 90.00
*R / R_free (%)*	19.7 / 28.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound) (pdb code 6an3). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound), PDB code: 6an3:

Copper binding site 1 out of 1 in 6an3

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Copper Binding Sites List in 6an3

Copper binding site 1 out of 1 in the Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound)

Mono view

Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu1001 b:62.8 occ:1.00	SD	A:MET314	2.3	45.9	1.0
	NE2	A:HIS244	2.4	48.1	1.0
	NE2	A:HIS242	2.5	30.6	1.0
	O	A:HOH1262	2.6	47.5	1.0
	O	A:HOH1276	3.1	41.7	1.0
	CD2	A:HIS244	3.2	45.9	1.0
	CD2	A:HIS242	3.3	31.7	1.0
	CE1	A:HIS244	3.5	49.2	1.0
	CG	A:MET314	3.6	42.6	1.0
	CE1	A:HIS242	3.6	31.7	1.0
	CE	A:MET314	3.8	46.2	1.0
	CB	A:MET314	4.2	37.9	1.0
	CG	A:HIS244	4.4	45.3	1.0
	CG	A:HIS242	4.5	29.5	1.0
	ND1	A:HIS244	4.5	51.4	1.0
	ND1	A:HIS242	4.6	30.8	1.0

Reference:

S.Maheshwari, C.Shimokawa, K.Rudzka, C.D.Kline, B.A.Eipper, R.E.Mains, S.B.Gabelli, N.Blackburn, L.M.Amzel. Effects of Copper Occupancy on the Conformational Landscape of Peptidylglycine Alpha-Hydroxylating Monooxygenase. Commun Biol V. 1 74 2018.
ISSN: ESSN 2399-3642
PubMed: 30271955
DOI: 10.1038/S42003-018-0082-Y

Page generated: Mon Jul 14 05:54:23 2025

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