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Sodium in PDB 1lla: Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation

Protein crystallography data

The structure of Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation, PDB code: 1lla was solved by B.Hazes, W.G.J.Hol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.18
Space group R 3 2
Cell size a, b, c (Å), α, β, γ (°) 117.002, 117.002, 117.002, 60.02, 60.02, 60.02
R / Rfree (%) 17.4 / n/a

Other elements in 1lla:

The structure of Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation also contains other interesting chemical elements:

Copper (Cu) 2 atoms
Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation (pdb code 1lla). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation, PDB code: 1lla:

Sodium binding site 1 out of 1 in 1lla

Go back to Sodium Binding Sites List in 1lla
Sodium binding site 1 out of 1 in the Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na631

b:17.5
occ:1.00
O A:SER507 2.3 8.0 1.0
O A:ASP578 2.3 12.9 1.0
O A:THR510 2.4 13.1 1.0
O A:HOH889 2.4 28.2 1.0
OD1 A:ASP578 2.8 25.8 1.0
O A:HOH875 3.0 44.1 1.0
C A:ASP578 3.3 13.7 1.0
C A:THR510 3.4 13.2 1.0
OG1 A:THR510 3.5 15.4 1.0
C A:SER507 3.5 10.1 1.0
N A:THR510 3.6 12.5 1.0
OG A:SER512 3.7 22.3 1.0
CG A:ASP578 3.7 20.9 1.0
CA A:THR510 3.9 12.6 1.0
CA A:ASP578 4.0 14.1 1.0
N A:ALA579 4.2 13.8 1.0
CA A:SER508 4.3 10.9 1.0
O A:ASP506 4.3 14.6 1.0
N A:SER508 4.3 10.0 1.0
CB A:THR510 4.3 10.7 1.0
CB A:ASP578 4.4 16.6 1.0
N A:SER512 4.4 20.2 1.0
C A:ASP506 4.4 14.6 1.0
C A:SER508 4.5 10.2 1.0
CA A:SER507 4.5 10.9 1.0
N A:SER507 4.5 13.2 1.0
CA A:ALA579 4.5 12.7 1.0
OD2 A:ASP578 4.5 24.0 1.0
N A:LEU511 4.5 14.5 1.0
N A:VAL509 4.7 10.9 1.0
C A:VAL509 4.7 11.6 1.0
C A:LEU511 4.8 18.7 1.0
O A:HOH820 4.8 33.7 1.0
CA A:LEU511 4.9 17.3 1.0
CB A:SER512 4.9 22.7 1.0
O A:LEU505 4.9 17.2 1.0
CB A:SER507 5.0 11.2 1.0

Reference:

B.Hazes, K.A.Magnus, C.Bonaventura, J.Bonaventura, Z.Dauter, K.H.Kalk, W.G.Hol. Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 A Resolution: Clues For A Mechanism For Allosteric Regulation. Protein Sci. V. 2 597 1993.
ISSN: ISSN 0961-8368
PubMed: 8518732
Page generated: Tue Dec 15 05:29:26 2020

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