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Copper in PDB 1lfi: Metal Substitution in Transferrins: the Crystal Structure of Human Copper-Lactoferrin at 2.1 Angstroms Resolution

Protein crystallography data

The structure of Metal Substitution in Transferrins: the Crystal Structure of Human Copper-Lactoferrin at 2.1 Angstroms Resolution, PDB code: 1lfi was solved by C.A.Smith, B.F.Anderson, H.M.Baker, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 155.900, 97.000, 56.000, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Metal Substitution in Transferrins: the Crystal Structure of Human Copper-Lactoferrin at 2.1 Angstroms Resolution (pdb code 1lfi). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Metal Substitution in Transferrins: the Crystal Structure of Human Copper-Lactoferrin at 2.1 Angstroms Resolution, PDB code: 1lfi:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1lfi

Go back to Copper Binding Sites List in 1lfi
Copper binding site 1 out of 2 in the Metal Substitution in Transferrins: the Crystal Structure of Human Copper-Lactoferrin at 2.1 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Metal Substitution in Transferrins: the Crystal Structure of Human Copper-Lactoferrin at 2.1 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu693

b:35.2
occ:1.00
O2 A:CO3695 1.9 31.1 1.0
OH A:TYR192 2.0 25.9 1.0
OD1 A:ASP60 2.0 34.1 1.0
NE2 A:HIS253 2.0 30.3 1.0
OH A:TYR92 2.8 28.0 1.0
CD2 A:HIS253 2.9 29.1 1.0
CE1 A:HIS253 3.0 30.6 1.0
CG A:ASP60 3.0 31.6 1.0
C A:CO3695 3.2 34.1 1.0
CZ A:TYR192 3.2 26.6 1.0
CB A:ASP60 3.5 29.0 1.0
NH2 A:ARG121 3.8 29.6 1.0
CZ A:TYR92 3.8 25.7 1.0
O1 A:CO3695 3.9 35.3 1.0
O3 A:CO3695 4.0 34.7 1.0
CE1 A:TYR192 4.0 26.5 1.0
CE2 A:TYR192 4.0 26.2 1.0
CG A:HIS253 4.1 29.8 1.0
NE A:ARG121 4.1 32.3 1.0
NH2 A:ARG210 4.1 21.0 1.0
ND1 A:HIS253 4.1 30.2 1.0
OD2 A:ASP60 4.1 34.2 1.0
CA A:ASP60 4.2 28.3 1.0
O A:HOH998 4.2 31.6 1.0
CZ A:ARG121 4.3 31.2 1.0
O A:HOH1219 4.5 39.5 1.0
CE1 A:TYR92 4.5 26.4 1.0
CE2 A:TYR92 4.7 24.4 1.0
OG1 A:THR122 4.9 28.5 1.0
CB A:THR122 4.9 28.8 1.0
N A:GLY61 4.9 28.2 1.0

Copper binding site 2 out of 2 in 1lfi

Go back to Copper Binding Sites List in 1lfi
Copper binding site 2 out of 2 in the Metal Substitution in Transferrins: the Crystal Structure of Human Copper-Lactoferrin at 2.1 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Metal Substitution in Transferrins: the Crystal Structure of Human Copper-Lactoferrin at 2.1 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu694

b:41.0
occ:1.00
OD1 A:ASP395 2.0 36.0 1.0
O2 A:CO3696 2.0 26.5 1.0
OH A:TYR435 2.0 30.1 1.0
NE2 A:HIS597 2.1 26.4 1.0
O1 A:CO3696 2.3 21.7 1.0
OH A:TYR528 2.3 29.1 1.0
C A:CO3696 2.5 24.7 1.0
CZ A:TYR435 3.0 29.9 1.0
CE1 A:HIS597 3.0 25.5 1.0
CD2 A:HIS597 3.1 26.4 1.0
CG A:ASP395 3.2 34.4 1.0
CZ A:TYR528 3.5 26.1 1.0
CE2 A:TYR435 3.5 29.6 1.0
O A:HOH997 3.7 29.5 1.0
NH2 A:ARG465 3.8 28.1 1.0
O3 A:CO3696 3.8 25.4 1.0
CB A:ASP395 3.9 30.5 1.0
CE1 A:TYR435 4.0 29.7 1.0
O A:HOH1122 4.0 30.7 1.0
ND1 A:HIS597 4.1 25.5 1.0
OD2 A:ASP395 4.2 36.0 1.0
CG A:HIS597 4.2 26.6 1.0
CE1 A:TYR528 4.2 23.7 1.0
CE2 A:TYR528 4.2 25.6 1.0
CA A:ASP395 4.6 28.9 1.0
CZ A:ARG465 4.6 28.5 1.0
NE A:ARG465 4.7 28.4 1.0
CD2 A:TYR435 4.7 29.6 1.0
N A:THR466 4.9 28.4 1.0
N A:ALA467 5.0 27.6 1.0

Reference:

C.A.Smith, B.F.Anderson, H.M.Baker, E.N.Baker. Metal Substitution in Transferrins: the Crystal Structure of Human Copper-Lactoferrin at 2.1-A Resolution. Biochemistry V. 31 4527 1992.
ISSN: ISSN 0006-2960
PubMed: 1581307
DOI: 10.1021/BI00133A020
Page generated: Thu Sep 3 16:07:06 2020
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