Structure of PDB 1yqt Chain A

Receptor sequence
>1yqtA (length=515) Species: 2261 (Pyrococcus furiosus) [Search protein sequence]
EEDCVHRYGVNAFVLYRLPVVKEGMVVGIVGPNGTGKSTAVKILAGQLIP
NLCGDNDSWDGVIRAFRGNELQNYFEKLKNGEIRPVVKPQYVDLIPKAVK
GKVIELLKKADETGKLEEVVKALELENVLEREIQHLSGGELQRVAIAAAL
LRNATFYFFDEPSSYLDIRQRLNAARAIRRLSEEGKSVLVVEHDLAVLDY
LSDIIHVVYGEPGVYGIFSQPKGTRNGINEFLRGYLKDENVRFRPYEIKF
TKTGERVEIERETLVTYPRLVKDYGSFRLEVEPGEIKKGEVIGIVGPNGI
GKTTFVKMLAGVEEPTEGKIEWDLTVAYKPQYIKADYEGTVYELLSKIDA
SKLNSNFYKTELLKPLGIIDLYDREVNELSGGELQRVAIAATLLRDADIY
LLDEPSAYLDVEQRLAVSRAIRHLMEKNEKTALVVEHDVLMIDYVSDRLM
VFEGEPGKYGRALPPMGMREGMNRFLASIGITFRRDPDTGRPRANKEGSV
KDREQKEKGEYYYIA
3D structure
PDB1yqt X-ray structure of RLI, an essential twin cassette ABC ATPase involved in ribosome biogenesis and HIV capsid assembly.
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 MG A T378 Q406 T303 Q331
BS02 MG A S113 Q165 S38 Q90
BS03 ADP A Y349 F352 N373 G374 I375 G376 K377 T378 T379 Y274 F277 N298 G299 I300 G301 K302 T303 T304
BS04 ADP A Y83 F88 N108 G109 G111 K112 S113 T114 Y8 F13 N33 G34 G36 K37 S38 T39
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity

View graph for
Molecular Function
External links
PDB RCSB:1yqt, PDBe:1yqt, PDBj:1yqt
PDBsum1yqt
PubMed15837203
UniProtQ8U306

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