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Chlorine in PDB 4g37: Structure of Cross-Linked Firefly Luciferase in Second Catalytic Conformation

Enzymatic activity of Structure of Cross-Linked Firefly Luciferase in Second Catalytic Conformation

All present enzymatic activity of Structure of Cross-Linked Firefly Luciferase in Second Catalytic Conformation:
1.13.12.7;

Protein crystallography data

The structure of Structure of Cross-Linked Firefly Luciferase in Second Catalytic Conformation, PDB code: 4g37 was solved by J.A.Sundlov, B.R.Branchini, A.M.Gulick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.22 / 2.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 75.638, 184.091, 170.530, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 25.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Cross-Linked Firefly Luciferase in Second Catalytic Conformation (pdb code 4g37). 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 Structure of Cross-Linked Firefly Luciferase in Second Catalytic Conformation, PDB code: 4g37:

Chlorine binding site 1 out of 1 in 4g37

Go back to Chlorine Binding Sites List in 4g37
Chlorine binding site 1 out of 1 in the Structure of Cross-Linked Firefly Luciferase in Second Catalytic Conformation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Cross-Linked Firefly Luciferase in Second Catalytic Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl603

b:76.7
occ:1.00
O B:HOH761 3.1 47.6 1.0
NH2 B:ARG261 3.5 41.8 1.0
ND2 B:ASN50 3.8 44.7 1.0
NH1 B:ARG261 4.3 43.5 1.0
CZ B:ARG261 4.4 47.3 1.0
CE1 B:TYR280 4.4 41.0 1.0
CG B:ASN50 4.9 42.9 1.0
CD1 B:TYR280 4.9 45.5 1.0

Reference:

J.A.Sundlov, D.M.Fontaine, T.L.Southworth, B.R.Branchini, A.M.Gulick. Crystal Structure of Firefly Luciferase in A Second Catalytic Conformation Supports A Domain Alternation Mechanism. Biochemistry V. 51 6493 2012.
ISSN: ISSN 0006-2960
PubMed: 22852753
DOI: 10.1021/BI300934S
Page generated: Sat Dec 12 10:38:34 2020

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