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Atomistry » Chlorine » PDB 4jk9-4jtg » 4jll » |
Chlorine in PDB 4jll: Crystal Structure of the Evolved Variant of the Computationally Designed Serine Hydrolase, OSH55.4_H1 Covalently Bound with Fp- Alkyne, Northeast Structural Genomics Consortium (Nesg) Target OR273Protein crystallography data
The structure of Crystal Structure of the Evolved Variant of the Computationally Designed Serine Hydrolase, OSH55.4_H1 Covalently Bound with Fp- Alkyne, Northeast Structural Genomics Consortium (Nesg) Target OR273, PDB code: 4jll
was solved by
A.Kuzin,
S.Lew,
S.Rajagopalan,
J.Seetharaman,
S.Tong,
J.K.Everett,
T.B.Acton,
D.Baker,
G.T.Montelione,
L.Tong,
J.F.Hunt,
Northeaststructural Genomics Consortium (Nesg),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the Evolved Variant of the Computationally Designed Serine Hydrolase, OSH55.4_H1 Covalently Bound with Fp- Alkyne, Northeast Structural Genomics Consortium (Nesg) Target OR273
(pdb code 4jll). 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 Crystal Structure of the Evolved Variant of the Computationally Designed Serine Hydrolase, OSH55.4_H1 Covalently Bound with Fp- Alkyne, Northeast Structural Genomics Consortium (Nesg) Target OR273, PDB code: 4jll: Chlorine binding site 1 out of 1 in 4jllGo back to Chlorine Binding Sites List in 4jll
Chlorine binding site 1 out
of 1 in the Crystal Structure of the Evolved Variant of the Computationally Designed Serine Hydrolase, OSH55.4_H1 Covalently Bound with Fp- Alkyne, Northeast Structural Genomics Consortium (Nesg) Target OR273
Mono view Stereo pair view
Reference:
S.Rajagopalan,
C.Wang,
K.Yu,
A.P.Kuzin,
F.Richter,
S.Lew,
A.E.Miklos,
M.L.Matthews,
J.Seetharaman,
M.Su,
J.F.Hunt,
B.F.Cravatt,
D.Baker.
Design of Activated Serine-Containing Catalytic Triads with Atomic-Level Accuracy. Nat.Chem.Biol. V. 10 386 2014.
Page generated: Sat Dec 12 10:48:27 2020
ISSN: ISSN 1552-4450 PubMed: 24705591 DOI: 10.1038/NCHEMBIO.1498 |
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