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Copper in PDB 3b1j: Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with CP12 in the Presence of Copper From Synechococcus Elongatus

Enzymatic activity of Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with CP12 in the Presence of Copper From Synechococcus Elongatus

All present enzymatic activity of Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with CP12 in the Presence of Copper From Synechococcus Elongatus:
1.2.1.13;

Protein crystallography data

The structure of Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with CP12 in the Presence of Copper From Synechococcus Elongatus, PDB code: 3b1j was solved by H.Matsumura, A.Kai, T.Inoue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 69.999, 161.603, 146.876, 90.00, 90.00, 90.00
R / Rfree (%) 23 / 27.5

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with CP12 in the Presence of Copper From Synechococcus Elongatus (pdb code 3b1j). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with CP12 in the Presence of Copper From Synechococcus Elongatus, PDB code: 3b1j:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3b1j

Go back to Copper Binding Sites List in 3b1j
Copper binding site 1 out of 2 in the Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with CP12 in the Presence of Copper From Synechococcus Elongatus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with CP12 in the Presence of Copper From Synechococcus Elongatus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu341

b:81.1
occ:1.00
SG A:CYS155 2.2 27.5 1.0
N A:THR156 2.5 30.5 1.0
O C:ASP75 2.6 63.0 1.0
OG1 A:THR156 2.6 32.8 1.0
N A:CYS155 3.2 30.1 1.0
CB A:THR156 3.3 31.1 1.0
C A:CYS155 3.3 30.4 1.0
CB A:CYS155 3.3 28.3 1.0
C C:ASP75 3.4 62.5 1.0
CA A:THR156 3.4 32.0 1.0
CA A:CYS155 3.4 29.8 1.0
CA C:ASP75 3.4 62.2 1.0
NE2 A:HIS182 3.8 24.5 1.0
CB A:SER154 4.0 31.4 1.0
OG A:SER154 4.1 32.3 1.0
O C:ASP74 4.1 58.8 1.0
C A:SER154 4.1 29.7 1.0
CD2 A:HIS182 4.2 21.5 1.0
CB C:ASP75 4.2 64.4 1.0
OH A:TYR316 4.3 16.2 1.0
CE2 A:TYR316 4.4 14.6 1.0
O A:CYS155 4.4 31.2 1.0
OD2 C:ASP75 4.5 68.1 1.0
N C:ASP75 4.5 60.0 1.0
CA A:SER154 4.6 30.9 1.0
C A:THR156 4.7 32.8 1.0
C C:ASP74 4.7 57.3 1.0
CG C:ASP75 4.7 67.1 1.0
CG2 A:THR156 4.8 31.3 1.0
N A:THR157 4.8 33.5 1.0
CZ A:TYR316 4.9 15.8 1.0
CE1 A:HIS182 4.9 23.0 1.0
O A:SER154 4.9 28.2 1.0

Copper binding site 2 out of 2 in 3b1j

Go back to Copper Binding Sites List in 3b1j
Copper binding site 2 out of 2 in the Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with CP12 in the Presence of Copper From Synechococcus Elongatus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with CP12 in the Presence of Copper From Synechococcus Elongatus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu341

b:61.0
occ:1.00
SG B:CYS155 2.0 29.5 1.0
N B:THR156 2.3 24.1 1.0
OG1 B:THR156 2.4 22.1 1.0
C B:CYS155 3.0 25.2 1.0
CB B:CYS155 3.0 27.4 1.0
CA B:THR156 3.1 23.9 1.0
N B:CYS155 3.2 27.4 1.0
CA B:CYS155 3.2 25.7 1.0
CB B:THR156 3.2 23.2 1.0
O D:ASP75 3.3 48.4 1.0
NE2 B:HIS182 3.6 17.8 1.0
OH B:TYR316 3.8 20.2 1.0
CE2 B:TYR316 3.8 14.9 1.0
CD2 B:HIS182 4.0 17.8 1.0
O B:CYS155 4.0 26.9 1.0
C B:SER154 4.1 28.5 1.0
OG B:SER154 4.2 28.4 1.0
C D:ASP75 4.2 48.0 1.0
CB B:SER154 4.2 28.7 1.0
CA D:ASP75 4.2 47.0 1.0
CZ B:TYR316 4.3 18.3 1.0
O D:ASP74 4.4 45.1 1.0
C B:THR156 4.5 26.0 1.0
CG2 B:THR156 4.5 20.0 1.0
N B:THR157 4.8 26.4 1.0
CA B:SER154 4.8 28.6 1.0
CE1 B:HIS182 4.8 18.0 1.0
O B:SER154 4.9 29.4 1.0
CD2 B:TYR316 5.0 16.3 1.0

Reference:

H.Matsumura, A.Kai, T.Maeda, M.Tamoi, A.Satoh, H.Tamura, M.Hirose, T.Ogawa, N.Kizu, A.Wadano, T.Inoue, S.Shigeoka. Structure Basis For the Regulation of Glyceraldehyde-3-Phosphate Dehydrogenase Activity Via the Intrinsically Disordered Protein CP12. Structure V. 19 1846 2011.
ISSN: ISSN 0969-2126
PubMed: 22153507
DOI: 10.1016/J.STR.2011.08.016
Page generated: Wed Jul 31 00:42:19 2024

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