Structure of PDB 6nab Chain A

Receptor sequence
>6nabA (length=496) Species: 5763 (Naegleria fowleri) [Search protein sequence]
EGIDVKKQENFSEWYSQVITKSEFLDYYDVSGCYIFRPNCWFVWESVQKF
FDAEIKKLGVQNVMFPLFVTKRALETEKDHVEGFSPEVAWVTKSGNSDLQ
EPIALRPTSETIMYPSYAKWIQSHRDLPLKLNQWTNVVRWEFKHAVPFIR
SREFYWQEGHSAFKSKEEADEEVFTILELYKRVYEELLAVPVIKGTKTEN
EKFAGADYTTTVETFIATNGRAVQGGTSHHLGQNFSKMFKIQFEAENKET
QFAYQNSWGLSTRTLGVMIMVHGDDKGMVLPPRVAFCQVVVIPLIDNATL
VEKTKEIYNELEKAGIRVKLDDRRTPGWKYNYWELRGVPLRIEVGPKDLE
KQQIMLCRRDTGEKWTMPLSEFSGDSIKAVLDKIHDSMLNKARKEMNERI
VVTRTWPEFIKALNSGNMCLIPWHESKAAEEYIKEKSKLESVQSQSDANT
GLTGAAKSLCVPLDQSSFPSLEGLENFYPEEAHKKPNCWALFGRSY
3D structure
PDB6nab Crystal structure of prolyl-tRNA synthetase from Naegleria fowleri in complex with proline and adenosine monophophsphate (AMP)
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.15: proline--tRNA 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 AMP A E144 I152 R153 S154 F157 Q227 T230 G262 S264 R266 E141 I149 R150 S151 F154 Q224 T227 G259 S261 R263
BS02 PRO A T111 E113 W159 E161 F206 H232 S260 W261 G262 T108 E110 W156 E158 F203 H229 S257 W258 G259
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004827 proline-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006433 prolyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0017101 aminoacyl-tRNA synthetase multienzyme complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6nab, PDBe:6nab, PDBj:6nab
PDBsum6nab
PubMed
UniProtA0A4V8H034

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