Structure of PDB 6uqo Chain F

Receptor sequence
>6uqoF (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.
ChainF
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 F L188 I189 R191 E215 S216 G217 V218 G219 K220 D396 L20 I21 R23 E47 S48 G49 V50 G51 K52 D228
BS02 ADP F T497 G498 V499 T502 V661 F665 A701 R702 T329 G330 V331 T334 V493 F497 A533 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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