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Zinc in PDB 3bp8: Crystal Structure of Mlc/Eiib Complex

Protein crystallography data

The structure of Crystal Structure of Mlc/Eiib Complex, PDB code: 3bp8 was solved by Y.J.An, H.I.Jung, S.S.Cha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.85
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 201.427, 55.424, 82.460, 90.00, 95.29, 90.00
R / Rfree (%) 22.8 / 30.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Mlc/Eiib Complex (pdb code 3bp8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Mlc/Eiib Complex, PDB code: 3bp8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3bp8

Go back to Zinc Binding Sites List in 3bp8
Zinc binding site 1 out of 2 in the Crystal Structure of Mlc/Eiib Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Mlc/Eiib Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn410

b:59.7
occ:1.00
SG A:CYS257 2.0 60.4 1.0
ND1 A:HIS247 2.1 28.3 1.0
SG A:CYS264 2.3 39.0 1.0
SG A:CYS259 2.4 50.8 1.0
CE1 A:HIS247 2.7 27.9 1.0
CB A:CYS264 2.9 38.0 1.0
CB A:CYS257 2.9 58.5 1.0
CG A:HIS247 3.2 28.8 1.0
CB A:CYS259 3.5 49.8 1.0
CB A:HIS247 3.7 31.4 1.0
NE2 A:HIS247 3.9 27.6 1.0
CD2 A:HIS247 4.1 27.9 1.0
CA A:HIS247 4.2 34.6 1.0
CA A:CYS264 4.3 38.5 1.0
CA A:CYS257 4.4 58.2 1.0
N A:CYS259 4.5 51.8 1.0
CA A:CYS259 4.7 50.0 1.0
N A:CYS264 4.9 39.4 1.0
C A:CYS257 4.9 56.2 1.0
O A:GLY246 4.9 32.8 1.0

Zinc binding site 2 out of 2 in 3bp8

Go back to Zinc Binding Sites List in 3bp8
Zinc binding site 2 out of 2 in the Crystal Structure of Mlc/Eiib Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Mlc/Eiib Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn407

b:45.7
occ:1.00
SG B:CYS264 2.0 31.6 1.0
SG B:CYS259 2.2 35.1 1.0
SG B:CYS257 2.3 32.3 1.0
ND1 B:HIS247 2.4 29.9 1.0
CB B:CYS257 2.8 30.7 1.0
CB B:CYS264 3.1 29.5 1.0
CE1 B:HIS247 3.1 29.7 1.0
CG B:HIS247 3.5 29.7 1.0
CB B:CYS259 3.5 29.0 1.0
CB B:HIS247 4.0 28.7 1.0
CA B:CYS257 4.2 31.1 1.0
NE2 B:HIS247 4.2 30.5 1.0
CB B:ASN261 4.3 31.6 1.0
N B:CYS259 4.3 28.5 1.0
CA B:HIS247 4.4 30.6 1.0
CD2 B:HIS247 4.5 30.9 1.0
CA B:CYS259 4.5 27.4 1.0
CA B:CYS264 4.5 28.6 1.0
C B:CYS257 4.6 30.0 1.0
N B:ASN261 4.6 28.9 1.0
C B:ASN261 4.7 29.3 1.0
CA B:ASN261 4.8 30.1 1.0
N B:CYS264 4.8 27.9 1.0
O B:ASN261 4.9 31.2 1.0
N B:HIS262 4.9 27.6 1.0
O B:CYS257 5.0 30.3 1.0
O B:HIS247 5.0 30.2 1.0
N B:TYR258 5.0 28.0 1.0

Reference:

T.W.Nam, H.I.Jung, Y.J.An, Y.H.Park, S.H.Lee, Y.J.Seok, S.S.Cha. Analyses of Mlc-Iibglc Interaction and A Plausible Molecular Mechanism of Mlc Inactivation By Membrane Sequestration Proc.Natl.Acad.Sci.Usa V. 105 3751 2008.
ISSN: ISSN 0027-8424
PubMed: 18319344
DOI: 10.1073/PNAS.0709295105
Page generated: Thu Oct 24 11:36:18 2024

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