Structure of PDB 4h2y Chain A

Receptor sequence
>4h2yA (length=295) Species: 224911 (Bradyrhizobium diazoefficiens USDA 110) [Search protein sequence]
DPLDHLADKLFHSMGSDGVYARTALYESIVERLAALITSHREAGTEALRF
PPVMSRAQLEKSGYLKSFPNLLGCVCGLHGTEREINAAVSRFDAGGDWTT
SLSPADLVLSPAACYPVYPIAASRGPLPKGGLRFDVAADCFRREPSKHLD
RLQSFRMREYVCIGTPDDVSDFRERWMVRAQAIARDLGLTFRVDYASDPF
FGRAGKMLANNQRDQQLKFELLIPLRSEEQPTACMSFNYHREHFGTTWGI
QDANGEPAHTGCVAFGMDRLAVAMFHTHGTDLSAWPAKVRDILGL
3D structure
PDB4h2y Adaptation of aminoacyl-tRNA synthetase catalytic core to carrier protein aminoacylation.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C131 R159 E161 R168 E176 K235 A250 S253 C279 R286
Catalytic site (residue number reindexed from 1) C114 R142 E144 R151 E159 K218 A233 S236 C262 R269
Enzyme Commision number 6.2.1.n2: amino acid--[acyl-carrier-protein] ligase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ZN A C131 E176 C279 C114 E159 C262
BS02 ATP A R159 R168 L169 F172 K235 A250 C251 G283 R286 R142 R151 L152 F155 K218 A233 C234 G266 R269
BS03 PNS A D215 N228 Q232 N255 H257 D198 N211 Q215 N238 H240
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation

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Molecular Function

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Biological Process
External links
PDB RCSB:4h2y, PDBe:4h2y, PDBj:4h2y
PDBsum4h2y
PubMed23541895
UniProtQ89VT8|AACL1_BRADU Amino acid--[acyl-carrier-protein] ligase 1 (Gene Name=bll0957)

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