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Chlorine in PDB 4fpd: Deprotonation of D96 in Bacteriorhodopsin Opens the Proton Uptake Pathway

Protein crystallography data

The structure of Deprotonation of D96 in Bacteriorhodopsin Opens the Proton Uptake Pathway, PDB code: 4fpd was solved by T.Wang, A.O.Sessions, C.S.Lunde, S.Rouani, R.M.Glaeser, M.T.Facciotti, Y.Duan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.95 / 2.65
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 60.931, 60.931, 107.701, 90.00, 90.00, 120.00
R / Rfree (%) 22.3 / 24

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Deprotonation of D96 in Bacteriorhodopsin Opens the Proton Uptake Pathway (pdb code 4fpd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Deprotonation of D96 in Bacteriorhodopsin Opens the Proton Uptake Pathway, PDB code: 4fpd:

Chlorine binding site 1 out of 1 in 4fpd

Go back to Chlorine Binding Sites List in 4fpd
Chlorine binding site 1 out of 1 in the Deprotonation of D96 in Bacteriorhodopsin Opens the Proton Uptake Pathway


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Deprotonation of D96 in Bacteriorhodopsin Opens the Proton Uptake Pathway within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:38.9
occ:1.00
NE1 A:TRP137 2.6 18.0 1.0
O A:HOH406 2.8 24.2 1.0
OG1 A:THR128 3.0 22.9 1.0
CD1 A:TRP137 3.5 14.9 1.0
CE2 A:TRP137 3.5 17.8 1.0
CG2 A:THR128 3.7 18.8 1.0
CZ2 A:TRP137 3.9 18.3 1.0
CB A:THR128 3.9 21.6 1.0
CG1 A:VAL124 4.4 18.8 1.0
CB A:TYR133 4.4 25.6 1.0
CD2 A:TYR133 4.6 29.2 1.0
CG A:TRP137 4.7 16.9 1.0
CD2 A:TRP137 4.7 17.8 1.0
CA A:THR128 4.8 21.9 1.0
CG A:TYR133 4.9 26.9 1.0

Reference:

T.Wang, A.O.Sessions, C.S.Lunde, S.Rouhani, R.M.Glaeser, Y.Duan, M.T.Facciotti. Deprotonation of D96 in Bacteriorhodopsin Opens the Proton Uptake Pathway. Structure V. 21 290 2013.
ISSN: ISSN 0969-2126
PubMed: 23394942
DOI: 10.1016/J.STR.2012.12.018
Page generated: Sun Jul 21 13:59:29 2024

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