Structure of PDB 6uqo Chain E

Receptor sequence
>6uqoE (length=578) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGV
GKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFK
ALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRV
IGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAH
HDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARLMPVSKRK
KTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIE
ALTEAIKMARAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLR
FDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEK
AHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIG
LIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVE
LQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLAN
ELLFGSLVDGGQVTVALDKEKNELTYGF
3D structure
PDB6uqo Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.
ChainE
Resolution3.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.21.92: endopeptidase Clp.
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 ADP E I189 V218 G219 T221 A222 D285 I357 P395 I21 V50 G51 T53 A54 D117 I189 P227
BS02 AGS E V460 F461 T497 G498 V499 G500 K501 T502 N606 L653 K664 R702 V292 F293 T329 G330 V331 G332 K333 T334 N438 L485 K496 R534
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity

View graph for
Molecular Function
External links
PDB RCSB:6uqo, PDBe:6uqo, PDBj:6uqo
PDBsum6uqo
PubMed32313240
UniProtP0ABH9|CLPA_ECOLI ATP-dependent Clp protease ATP-binding subunit ClpA (Gene Name=clpA)

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