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Copper in PDB 5nlp: Auxiliary Activity 9

Protein crystallography data

The structure of Auxiliary Activity 9, PDB code: 5nlp was solved by K.E.H.Frandsen, J.-C.N.Poulsen, T.Tandrup, L.Lo Leggio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.20 / 1.59
Space group P 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 125.008, 125.008, 125.008, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 17.6

Copper Binding Sites:

The binding sites of Copper atom in the Auxiliary Activity 9 (pdb code 5nlp). 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 Auxiliary Activity 9, PDB code: 5nlp:

Copper binding site 1 out of 1 in 5nlp

Go back to Copper Binding Sites List in 5nlp
Copper binding site 1 out of 1 in the Auxiliary Activity 9


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Auxiliary Activity 9 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:24.5
occ:1.00
ND1 A:HIC1 1.9 21.5 1.0
NE2 A:HIS78 2.0 23.9 1.0
N A:HIC1 2.2 20.4 1.0
OH A:TYR164 2.8 20.2 1.0
CE1 A:HIC1 2.9 23.8 1.0
CG A:HIC1 2.9 21.4 1.0
CD2 A:HIS78 3.0 21.1 1.0
CE1 A:HIS78 3.0 25.6 1.0
CA A:HIC1 3.2 19.0 1.0
CB A:HIC1 3.4 19.3 1.0
O A:HOH613 3.6 33.2 1.0
OE1 A:GLN162 3.8 22.9 1.0
CZ A:TYR164 3.8 17.5 1.0
NE2 A:HIC1 4.0 23.8 1.0
CD2 A:HIC1 4.1 21.1 1.0
ND1 A:HIS78 4.1 27.1 1.0
O A:HOH498 4.1 26.2 1.0
CG A:HIS78 4.1 22.3 1.0
O A:HOH563 4.1 28.0 1.0
CE1 A:TYR164 4.5 16.4 1.0
CE2 A:TYR164 4.6 16.7 1.0
C A:HIC1 4.6 19.3 1.0
CD A:GLN162 4.8 23.1 1.0

Reference:

T.J.Simmons, K.E.H.Frandsen, L.Ciano, T.Tryfona, N.Lenfant, J.C.Poulsen, L.F.L.Wilson, T.Tandrup, M.Tovborg, K.Schnorr, K.S.Johansen, B.Henrissat, P.H.Walton, L.Lo Leggio, P.Dupree. Structural and Electronic Determinants of Lytic Polysaccharide Monooxygenase Reactivity on Polysaccharide Substrates. Nat Commun V. 8 1064 2017.
ISSN: ESSN 2041-1723
PubMed: 29057953
DOI: 10.1038/S41467-017-01247-3
Page generated: Sun Dec 13 11:19:00 2020

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