Structure of PDB 4bev Chain A

Receptor sequence
>4bevA (length=663) Species: 446 (Legionella pneumophila) [Search protein sequence]
VSPEYLDMRRRFWIALMLTIPVVILEMGGHGLKHFISGNGSSWIQLLLAT
PVVLWGGWPFFKRGWQSLKTGQLNMFTLIAMGIGVAWIYSMVAVLWPGVF
PHAFRSQEGVVAVYFEAAAVITTLVLLGQVLELKAREQTGSAIRALLKLV
PESAHRIKEDGSEEEVSLDNVAVGDLLRVRPGEKIPVDGEVQEGRSFVDE
SMVTGEPIPVAKEASAKVIGATINQTGSFVMKALHVGSDTMLARIVQMVS
DAQRSRAPIQRLADTVSGWFVPAVILVAVLSFIVWALLGPQPALSYGLIA
AVSVLIIACPCALGLATPMSIMVGVGKGAQSGVLIKNAEALERMEKVNTL
VVDKTGTLTEGHPKLTRIVTDDFVEDNALALAAALEHQSEHPLANAIVHA
AKEKGLSLGSVEAFEAPTGKGVVGQVDGHHVAIGNARLMQEHGGDNAPLF
EKADELRGKGASVMFMAVDGKTVALLVVEDPIKSSTPETILELQQSGIEI
VMLTGDSKRTAEAVAGTLGIKKVVAEIMPEDKSRIVSELKDKGLIVAMAG
DGVNDAPALAKADIGIAMGTGTDVAIESAGVTLLHGDLRGIAKARRLSES
TMSNIRQNLFFAFIYNVLGVPLAAGVLYPLTGLLLSPMIAAAAMALSSVS
VIINALRLKRVTL
3D structure
PDB4bev ATPase Crystal Structure with Bound Phosphate Analogue
ChainA
Resolution3.583 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D426 D624 D628
Catalytic site (residue number reindexed from 1) D353 D551 D555
Enzyme Commision number 7.2.2.8: P-type Cu(+) transporter.
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 D426 T428 D624 D353 T355 D551
BS02 MGF A D426 K427 T428 T577 D353 K354 T355 T504
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0005215 transporter activity
GO:0005507 copper ion binding
GO:0005524 ATP binding
GO:0015662 P-type ion transporter activity
GO:0016887 ATP hydrolysis activity
GO:0019829 ATPase-coupled monoatomic cation transmembrane transporter activity
GO:0043682 P-type divalent copper transporter activity
GO:0046872 metal ion binding
GO:0140581 P-type monovalent copper transporter activity
Biological Process
GO:0006812 monoatomic cation transport
GO:0006825 copper ion transport
GO:0006878 intracellular copper ion homeostasis
GO:0055070 copper ion homeostasis
GO:0060003 copper ion export
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4bev, PDBe:4bev, PDBj:4bev
PDBsum4bev
PubMed
UniProtQ5ZWR1|COPA_LEGPH Copper-exporting P-type ATPase (Gene Name=copA)

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