4BEV

ATPase crystal structure with bound phosphate analogue

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0005215	molecular_function	transporter activity
A	0005507	molecular_function	copper ion binding
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0006812	biological_process	monoatomic cation transport
A	0006825	biological_process	copper ion transport
A	0006878	biological_process	intracellular copper ion homeostasis
A	0015662	molecular_function	P-type ion transporter activity
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0019829	molecular_function	ATPase-coupled monoatomic cation transmembrane transporter activity
A	0043682	molecular_function	P-type divalent copper transporter activity
A	0046872	molecular_function	metal ion binding
A	0055070	biological_process	copper ion homeostasis
A	0060003	biological_process	copper ion export
A	0140581	molecular_function	P-type monovalent copper transporter activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 900

Chain	Residue
A	ASP426
A	THR428
A	ASP624
A	MGF950
A	HOH2002

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site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MGF A 950

Chain	Residue
A	LEU576
A	THR577
A	GLY578
A	LYS605
A	ASN627
A	MG900
A	HOH2001
A	THR277
A	ASP426
A	LYS427
A	THR428

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Functional Information from PROSITE/UniProt

site_id	PS00154
Number of Residues	7
Details	ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT

Chain	Residue	Details
A	ASP426-THR432

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	160
Details	TRANSMEM: Helical => ECO:0000255

Chain	Residue	Details
A	PHE85-LEU105
A	SER114-PHE134
A	PHE149-TRP169
A	VAL183-VAL203
A	GLY341-LEU361
A	TYR369-ALA389
A	LEU682-PRO702
A	LEU706-ILE726

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: 4-aspartylphosphate intermediate => ECO:0000305|Ref.4, ECO:0000305|Ref.5

Chain	Residue	Details
A	ASP426

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:24317491, ECO:0000269|Ref.4, ECO:0000269|Ref.5, ECO:0007744|PDB:4BBJ, ECO:0007744|PDB:4BEV, ECO:0007744|PDB:4BYG

Chain	Residue	Details
A	ASP426
A	THR428
A	ASP624

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site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Important for copper transport => ECO:0000303|PubMed:24317491

Chain	Residue	Details
A	GLU189
A	CYS382
A	CYS384
A	MET717

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