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Copper in PDB 6ala: Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate

Enzymatic activity of Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate

All present enzymatic activity of Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate:
1.14.17.3; 4.3.2.5;

Protein crystallography data

The structure of Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate, PDB code: 6ala 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) 29.05 / 2.59
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 171.370, 52.462, 116.457, 90.00, 128.74, 90.00
R / Rfree (%) 17.8 / 23.8

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate (pdb code 6ala). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate, PDB code: 6ala:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 6ala

Go back to Copper Binding Sites List in 6ala
Copper binding site 1 out of 2 in the Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate


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 H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:32.8
occ:1.00
OB1 A:FLC1002 2.0 27.5 1.0
NE2 A:HIS244 2.2 27.2 1.0
NE2 A:HIS107 2.2 27.2 1.0
NE2 A:HIS242 2.3 29.7 1.0
OHB A:FLC1002 2.5 29.9 1.0
CBC A:FLC1002 3.0 30.8 1.0
CD2 A:HIS244 3.0 27.9 1.0
CE1 A:HIS242 3.1 29.9 1.0
CE1 A:HIS107 3.2 29.8 1.0
CD2 A:HIS107 3.2 28.2 1.0
CE1 A:HIS244 3.2 27.5 1.0
CB A:FLC1002 3.3 31.3 1.0
CD2 A:HIS242 3.4 29.8 1.0
O A:HOH1140 3.8 36.9 1.0
OA1 A:FLC1002 4.0 35.4 1.0
OB2 A:FLC1002 4.1 29.5 1.0
CG A:HIS244 4.2 26.6 1.0
OG1 A:FLC1002 4.2 30.2 1.0
ND1 A:HIS244 4.2 27.6 1.0
CG A:FLC1002 4.2 30.6 1.0
ND1 A:HIS107 4.3 30.4 1.0
ND1 A:HIS242 4.3 29.6 1.0
CG A:MET314 4.3 28.4 1.0
CG A:HIS107 4.4 27.4 1.0
CA A:FLC1002 4.5 32.8 1.0
CG A:HIS242 4.5 27.5 1.0
CAC A:FLC1002 4.6 34.8 1.0
CGC A:FLC1002 4.7 31.1 1.0
CB A:MET314 4.8 26.7 1.0
ND1 A:HIS172 5.0 19.5 1.0

Copper binding site 2 out of 2 in 6ala

Go back to Copper Binding Sites List in 6ala
Copper binding site 2 out of 2 in the Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu1001

b:35.5
occ:1.00
OA2 C:FLC1002 1.9 52.4 1.0
NE2 C:HIS244 2.2 21.2 1.0
NE2 C:HIS242 2.3 21.5 1.0
NE2 C:HIS107 2.4 22.5 1.0
CAC C:FLC1002 2.5 53.8 1.0
CG C:FLC1002 2.8 35.0 1.0
CD2 C:HIS244 3.0 22.1 1.0
CE1 C:HIS242 3.1 22.1 1.0
OA1 C:FLC1002 3.2 62.8 1.0
CD2 C:HIS107 3.3 21.7 1.0
CE1 C:HIS244 3.3 21.5 1.0
CE1 C:HIS107 3.4 23.0 1.0
CA C:FLC1002 3.4 43.0 1.0
CD2 C:HIS242 3.4 22.0 1.0
CB C:FLC1002 3.4 39.9 1.0
CBC C:FLC1002 3.9 38.0 1.0
OB1 C:FLC1002 4.0 33.8 1.0
CGC C:FLC1002 4.1 34.7 1.0
ND1 C:HIS242 4.2 21.5 1.0
CG C:HIS244 4.2 23.1 1.0
ND1 C:HIS244 4.3 23.0 1.0
CG C:HIS242 4.4 21.3 1.0
OG2 C:FLC1002 4.4 35.6 1.0
CG C:HIS107 4.5 22.0 1.0
ND1 C:HIS107 4.5 23.2 1.0
CB C:MET314 4.6 31.6 1.0
OHB C:FLC1002 4.8 47.9 1.0
CG C:MET314 4.8 35.0 1.0
ND1 C:HIS172 4.9 20.7 1.0
OB2 C:FLC1002 4.9 33.2 1.0
CE1 C:HIS172 4.9 20.6 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 05:53:49 2025

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