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Copper in PDB 3nsd: Silver Bound to the Multicopper Oxidase Cueo (Untagged)

Protein crystallography data

The structure of Silver Bound to the Multicopper Oxidase Cueo (Untagged), PDB code: 3nsd was solved by W.R.Montfort, S.A.Roberts, S.K.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.40 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 50.181, 90.324, 53.810, 90.00, 102.26, 90.00
R / Rfree (%) 18.7 / 23.8

Other elements in 3nsd:

The structure of Silver Bound to the Multicopper Oxidase Cueo (Untagged) also contains other interesting chemical elements:

Silver (Ag) 3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Silver Bound to the Multicopper Oxidase Cueo (Untagged) (pdb code 3nsd). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Silver Bound to the Multicopper Oxidase Cueo (Untagged), PDB code: 3nsd:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 3nsd

Go back to Copper Binding Sites List in 3nsd
Copper binding site 1 out of 4 in the Silver Bound to the Multicopper Oxidase Cueo (Untagged)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Silver Bound to the Multicopper Oxidase Cueo (Untagged) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu601

b:38.7
occ:1.00
NE2 A:HIS446 2.1 39.7 1.0
NE2 A:HIS101 2.1 39.0 1.0
O A:HOH16 2.6 43.6 1.0
CD2 A:HIS446 3.0 40.2 1.0
CD2 A:HIS101 3.0 38.2 1.0
CE1 A:HIS101 3.1 38.4 1.0
CE1 A:HIS446 3.2 41.6 1.0
NE2 A:HIS448 3.2 43.1 1.0
CD2 A:HIS448 3.3 40.7 1.0
CG A:HIS103 3.5 36.4 1.0
CA A:HIS103 3.6 37.4 1.0
O A:O801 3.6 45.9 1.0
CU A:CU602 3.6 44.4 1.0
ND1 A:HIS103 3.7 37.6 1.0
CB A:HIS103 3.7 37.8 1.0
CE1 A:HIS448 3.9 44.2 1.0
CG A:HIS448 3.9 42.1 1.0
CD2 A:HIS103 4.1 36.8 1.0
CU A:CU603 4.1 40.1 1.0
CG A:HIS446 4.2 39.3 1.0
CG A:HIS101 4.2 36.9 1.0
ND1 A:HIS448 4.2 40.8 1.0
ND1 A:HIS101 4.2 36.3 1.0
ND1 A:HIS446 4.2 40.5 1.0
CE1 A:HIS103 4.2 35.0 1.0
N A:GLY104 4.3 38.9 1.0
NE2 A:HIS103 4.4 35.3 1.0
C A:HIS103 4.5 37.9 1.0
N A:HIS103 4.5 38.4 1.0
CA A:HIS448 4.6 40.9 1.0
O A:HOH8 4.8 40.4 1.0
CB A:HIS448 4.8 41.4 1.0
O A:HOH540 4.8 54.3 1.0
O A:TRP102 4.8 37.9 1.0

Copper binding site 2 out of 4 in 3nsd

Go back to Copper Binding Sites List in 3nsd
Copper binding site 2 out of 4 in the Silver Bound to the Multicopper Oxidase Cueo (Untagged)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Silver Bound to the Multicopper Oxidase Cueo (Untagged) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu602

b:44.4
occ:1.00
NE2 A:HIS499 2.1 37.5 1.0
NE2 A:HIS143 2.1 40.7 1.0
NE2 A:HIS448 2.2 43.1 1.0
O A:O801 2.3 45.9 1.0
CD2 A:HIS499 3.0 39.7 1.0
CD2 A:HIS143 3.0 41.0 1.0
CE1 A:HIS499 3.0 40.0 1.0
CE1 A:HIS143 3.1 40.0 1.0
CE1 A:HIS448 3.2 44.2 1.0
CD2 A:HIS448 3.2 40.7 1.0
O A:HOH735 3.5 57.1 1.0
CU A:CU601 3.6 38.7 1.0
CD2 A:HIS446 3.8 40.2 1.0
CD2 A:HIS101 4.1 38.2 1.0
NE2 A:HIS101 4.1 39.0 1.0
ND1 A:HIS499 4.1 38.9 1.0
CG A:HIS499 4.2 38.9 1.0
ND1 A:HIS143 4.2 40.4 1.0
CG A:HIS143 4.2 41.3 1.0
ND1 A:HIS448 4.3 40.8 1.0
CU A:CU603 4.3 40.1 1.0
NE2 A:HIS446 4.3 39.7 1.0
CG A:HIS448 4.3 42.1 1.0
CB A:MET497 4.7 39.1 1.0
CE1 A:HIS141 4.7 34.1 1.0
CE1 A:HIS101 4.8 38.4 1.0
OE1 A:GLU506 4.8 49.1 1.0
CG A:HIS101 4.8 36.9 1.0
CD2 A:HIS501 5.0 37.7 1.0
NE2 A:HIS141 5.0 34.5 1.0

Copper binding site 3 out of 4 in 3nsd

Go back to Copper Binding Sites List in 3nsd
Copper binding site 3 out of 4 in the Silver Bound to the Multicopper Oxidase Cueo (Untagged)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Silver Bound to the Multicopper Oxidase Cueo (Untagged) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu603

b:40.1
occ:1.00
O A:O801 2.1 45.9 1.0
NE2 A:HIS141 2.1 34.5 1.0
ND1 A:HIS103 2.1 37.6 1.0
NE2 A:HIS501 2.2 37.4 1.0
CE1 A:HIS141 3.0 34.1 1.0
CE1 A:HIS103 3.1 35.0 1.0
CD2 A:HIS141 3.1 34.5 1.0
CG A:HIS103 3.1 36.4 1.0
CD2 A:HIS501 3.1 37.7 1.0
CE1 A:HIS501 3.3 36.0 1.0
CB A:HIS103 3.4 37.8 1.0
CZ2 A:TRP139 3.8 36.2 1.0
O A:HOH735 4.0 57.1 1.0
ND1 A:HIS141 4.1 33.5 1.0
CU A:CU601 4.1 38.7 1.0
NE2 A:HIS103 4.2 35.3 1.0
CG A:HIS141 4.2 35.4 1.0
CE2 A:TRP139 4.2 33.8 1.0
CD2 A:HIS103 4.2 36.8 1.0
CU A:CU602 4.3 44.4 1.0
CG A:HIS501 4.3 37.1 1.0
CD2 A:HIS101 4.3 38.2 1.0
ND1 A:HIS501 4.4 34.7 1.0
NE1 A:TRP139 4.4 37.0 1.0
CD2 A:HIS446 4.4 40.2 1.0
CH2 A:TRP139 4.5 34.0 1.0
NE2 A:HIS446 4.6 39.7 1.0
CA A:HIS103 4.7 37.4 1.0
NE2 A:HIS101 4.8 39.0 1.0

Copper binding site 4 out of 4 in 3nsd

Go back to Copper Binding Sites List in 3nsd
Copper binding site 4 out of 4 in the Silver Bound to the Multicopper Oxidase Cueo (Untagged)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Silver Bound to the Multicopper Oxidase Cueo (Untagged) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu604

b:39.2
occ:1.00
ND1 A:HIS443 2.0 41.4 1.0
SG A:CYS500 2.2 39.5 1.0
ND1 A:HIS505 2.2 37.8 1.0
CG A:HIS443 3.0 40.1 1.0
CE1 A:HIS443 3.1 40.4 1.0
CG A:HIS505 3.1 37.3 1.0
CB A:CYS500 3.2 38.8 1.0
CE1 A:HIS505 3.2 38.5 1.0
CB A:HIS443 3.2 41.5 1.0
SD A:MET510 3.3 41.3 1.0
CB A:HIS505 3.4 38.5 1.0
CA A:HIS443 3.6 41.6 1.0
O A:LEU442 3.6 42.7 1.0
CD2 A:HIS443 4.1 37.1 1.0
NE2 A:HIS443 4.2 39.3 1.0
CB A:LEU502 4.2 34.2 1.0
CE A:MET510 4.3 37.3 1.0
CD2 A:HIS505 4.3 36.7 1.0
C A:LEU442 4.3 42.0 1.0
NE2 A:HIS505 4.3 35.6 1.0
N A:HIS443 4.3 41.8 1.0
CA A:CYS500 4.6 38.9 1.0
CG A:MET510 4.8 38.6 1.0
C A:HIS443 4.9 41.3 1.0
CA A:HIS505 4.9 39.0 1.0
O A:LEU502 4.9 35.6 1.0
CD1 A:LEU502 4.9 34.6 1.0
N A:LEU502 5.0 35.5 1.0

Reference:

S.K.Singh, S.A.Roberts, S.F.Mcdevitt, A.Weichsel, G.F.Wildner, G.B.Grass, C.Rensing, W.R.Montfort. Crystal Structures of Multicopper Oxidase Cueo Bound to Copper(I) and Silver(I): Functional Role of A Methionine-Rich Sequence. J. Biol. Chem. V. 286 37849 2011.
ISSN: ESSN 1083-351X
PubMed: 21903583
DOI: 10.1074/JBC.M111.293589
Page generated: Sun Dec 13 11:11:04 2020

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