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Copper in PDB 1ntd: Structure of Alcaligenes Faecalis Nitrite Reductase Mutant M150E That Contains Zinc

Enzymatic activity of Structure of Alcaligenes Faecalis Nitrite Reductase Mutant M150E That Contains Zinc

All present enzymatic activity of Structure of Alcaligenes Faecalis Nitrite Reductase Mutant M150E That Contains Zinc:
1.7.99.3;

Protein crystallography data

The structure of Structure of Alcaligenes Faecalis Nitrite Reductase Mutant M150E That Contains Zinc, PDB code: 1ntd was solved by M.E.P.Murphy, E.T.Adman, S.Turley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.30
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 127.760, 127.760, 67.020, 90.00, 90.00, 120.00
R / Rfree (%) 17.2 / 23.2

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Alcaligenes Faecalis Nitrite Reductase Mutant M150E That Contains Zinc (pdb code 1ntd). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structure of Alcaligenes Faecalis Nitrite Reductase Mutant M150E That Contains Zinc, PDB code: 1ntd:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1ntd

Go back to Copper Binding Sites List in 1ntd
Copper binding site 1 out of 2 in the Structure of Alcaligenes Faecalis Nitrite Reductase Mutant M150E That Contains Zinc


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Alcaligenes Faecalis Nitrite Reductase Mutant M150E That Contains Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:19.5
occ:1.00
OE1 A:GLU150 2.0 12.9 1.0
ND1 A:HIS95 2.0 14.9 1.0
ND1 A:HIS145 2.0 12.9 1.0
SG A:CYS136 2.2 13.4 1.0
CD A:GLU150 2.7 13.1 1.0
OE2 A:GLU150 2.8 18.3 1.0
CE1 A:HIS95 2.9 12.0 1.0
CE1 A:HIS145 2.9 10.9 1.0
CG A:HIS95 3.1 10.3 1.0
CB A:CYS136 3.1 15.8 1.0
CG A:HIS145 3.2 13.3 1.0
CB A:HIS95 3.5 11.6 1.0
CB A:HIS145 3.6 12.5 1.0
CA A:HIS95 3.9 10.0 1.0
CG A:PRO138 4.0 19.0 1.0
NE2 A:HIS95 4.1 13.5 1.0
CG A:GLU150 4.1 11.7 1.0
CD2 A:HIS95 4.1 10.3 1.0
NE2 A:HIS145 4.1 7.0 1.0
CD2 A:HIS145 4.2 9.8 1.0
O A:MET94 4.3 9.7 1.0
SD A:MET62 4.3 18.0 1.0
CD A:PRO138 4.5 18.6 1.0
CB A:GLU150 4.6 9.4 1.0
CA A:CYS136 4.6 16.7 1.0
CA A:HIS145 4.8 13.9 1.0
N A:ASN96 4.8 15.0 1.0
CB A:MET62 4.9 14.2 1.0
C A:HIS95 4.9 12.9 1.0
N A:HIS95 5.0 8.4 1.0

Copper binding site 2 out of 2 in 1ntd

Go back to Copper Binding Sites List in 1ntd
Copper binding site 2 out of 2 in the Structure of Alcaligenes Faecalis Nitrite Reductase Mutant M150E That Contains Zinc


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of Alcaligenes Faecalis Nitrite Reductase Mutant M150E That Contains Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:16.3
occ:1.00
NE2 A:HIS100 2.0 2.0 1.0
O A:HOH503 2.1 12.0 1.0
NE2 A:HIS135 2.3 12.9 1.0
CE1 A:HIS100 2.9 2.0 1.0
CD2 A:HIS100 3.1 2.0 1.0
CE1 A:HIS135 3.3 8.9 1.0
CD2 A:HIS135 3.3 12.4 1.0
OD2 A:ASP98 3.8 17.0 1.0
ND1 A:HIS100 4.1 2.0 1.0
CG A:HIS100 4.2 2.0 1.0
CG A:ASP98 4.3 10.7 1.0
ND1 A:HIS135 4.4 11.8 1.0
CG A:HIS135 4.4 11.7 1.0
OD1 A:ASP98 4.5 12.2 1.0

Reference:

M.E.Murphy, S.Turley, M.Kukimoto, M.Nishiyama, S.Horinouchi, H.Sasaki, M.Tanokura, E.T.Adman. Structure of Alcaligenes Faecalis Nitrite Reductase and A Copper Site Mutant, M150E, That Contains Zinc. Biochemistry V. 34 12107 1995.
ISSN: ISSN 0006-2960
PubMed: 7547950
DOI: 10.1021/BI00038A003
Page generated: Wed Oct 28 14:16:17 2020
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