Atomistry » Copper » PDB 5zpq-6fok » 6ala
Atomistry »
  Copper »
    PDB 5zpq-6fok »
      6ala »

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: Sun Dec 13 11:21:59 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy