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PDBsum entry 3pco
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242 a.a.
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795 a.a.
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323 a.a.
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* Residue conservation analysis
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PDB id:
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Ligase
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Title:
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Crystal structure of e. Coli phenylalanine-tRNA synthetase complexed with phenylalanine and amp
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Structure:
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Phenylalanyl-tRNA synthetase, alpha subunit. Chain: a, c. Fragment: ligase. Engineered: yes. Phenylalanyl-tRNA synthetase, beta chain. Chain: b, d. Engineered: yes
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Source:
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Escherichia coli. Organism_taxid: 562. Gene: ecdh1_1928. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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3.02Å
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R-factor:
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0.235
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R-free:
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0.300
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Authors:
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I.Mermershtain,I.Finarov,L.Klipcan,N.Kessler,H.Rozenberg,M.G.Safro
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Key ref:
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I.Mermershtain
et al.
(2011).
Idiosyncrasy and identity in the prokaryotic Phe-system: crystal structure of E. coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP.
Protein Sci,
20,
160-167.
PubMed id:
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Date:
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21-Oct-10
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Release date:
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02-Mar-11
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PROCHECK
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Headers
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References
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P08312
(SYFA_ECOLI) -
Phenylalanine--tRNA ligase alpha subunit from Escherichia coli (strain K12)
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Seq: Struc:
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327 a.a.
242 a.a.
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Enzyme class:
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Chains A, B, C, D:
E.C.6.1.1.20
- phenylalanine--tRNA ligase.
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Reaction:
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tRNA(Phe) + L-phenylalanine + ATP = L-phenylalanyl-tRNA(Phe) + AMP + diphosphate + H+
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tRNA(Phe)
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L-phenylalanine
Bound ligand (Het Group name = )
corresponds exactly
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ATP
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=
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L-phenylalanyl-tRNA(Phe)
Bound ligand (Het Group name = )
corresponds exactly
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+
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AMP
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+
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diphosphate
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Protein Sci
20:160-167
(2011)
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PubMed id:
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Idiosyncrasy and identity in the prokaryotic Phe-system: crystal structure of E. coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP.
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I.Mermershtain,
I.Finarov,
L.Klipcan,
N.Kessler,
H.Rozenberg,
M.G.Safro.
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ABSTRACT
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');
}
}
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