Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7BT2

Crystal structure of the SERCA2a in the E2.ATP state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000045	biological_process	autophagosome assembly
A	0000166	molecular_function	nucleotide binding
A	0002026	biological_process	regulation of the force of heart contraction
A	0003012	biological_process	muscle system process
A	0005215	molecular_function	transporter activity
A	0005246	molecular_function	calcium channel regulator activity
A	0005388	molecular_function	P-type calcium transporter activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005886	cellular_component	plasma membrane
A	0006811	biological_process	monoatomic ion transport
A	0006816	biological_process	calcium ion transport
A	0006874	biological_process	intracellular calcium ion homeostasis
A	0006937	biological_process	regulation of muscle contraction
A	0006984	biological_process	ER-nucleus signaling pathway
A	0007155	biological_process	cell adhesion
A	0008544	biological_process	epidermis development
A	0010460	biological_process	positive regulation of heart rate
A	0010666	biological_process	positive regulation of cardiac muscle cell apoptotic process
A	0010882	biological_process	regulation of cardiac muscle contraction by calcium ion signaling
A	0014883	biological_process	transition between fast and slow fiber
A	0014898	biological_process	cardiac muscle hypertrophy in response to stress
A	0016020	cellular_component	membrane
A	0016240	biological_process	autophagosome membrane docking
A	0016529	cellular_component	sarcoplasmic reticulum
A	0016887	molecular_function	ATP hydrolysis activity
A	0019899	molecular_function	enzyme binding
A	0031095	cellular_component	platelet dense tubular network membrane
A	0032469	biological_process	endoplasmic reticulum calcium ion homeostasis
A	0032470	biological_process	positive regulation of endoplasmic reticulum calcium ion concentration
A	0033017	cellular_component	sarcoplasmic reticulum membrane
A	0033292	biological_process	T-tubule organization
A	0034220	biological_process	monoatomic ion transmembrane transport
A	0034599	biological_process	cellular response to oxidative stress
A	0034976	biological_process	response to endoplasmic reticulum stress
A	0044325	molecular_function	transmembrane transporter binding
A	0044548	molecular_function	S100 protein binding
A	0045822	biological_process	negative regulation of heart contraction
A	0046872	molecular_function	metal ion binding
A	0070050	biological_process	neuron cellular homeostasis
A	0070296	biological_process	sarcoplasmic reticulum calcium ion transport
A	0070588	biological_process	calcium ion transmembrane transport
A	0086036	biological_process	regulation of cardiac muscle cell membrane potential
A	0086039	molecular_function	P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential
A	0097470	cellular_component	ribbon synapse
A	0098909	biological_process	regulation of cardiac muscle cell action potential involved in regulation of contraction
A	0106222	molecular_function	lncRNA binding
A	0140056	biological_process	organelle localization by membrane tethering
A	1903233	biological_process	regulation of calcium ion-dependent exocytosis of neurotransmitter
A	1903515	biological_process	calcium ion transport from cytosol to endoplasmic reticulum
A	1903779	biological_process	regulation of cardiac conduction
A	1990036	biological_process	calcium ion import into sarcoplasmic reticulum
A	1990456	biological_process	mitochondrion-endoplasmic reticulum membrane tethering

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue ATP A 1001

Chain	Residue
A	ASP351
A	LYS514
A	GLY515
A	ALA516
A	ARG559
A	LEU561
A	THR624
A	GLY625
A	ASP626
A	ARG677
A	HOH1104
A	LYS352
A	HOH1164
A	HOH1170
A	THR353
A	GLU439
A	GLU442
A	PHE487
A	ARG489
A	LYS492
A	MET494

site_id	AC2
Number of Residues	4
Details	binding site for residue K A 1002

Chain	Residue
A	LEU710
A	LYS711
A	ALA713
A	GLU731

site_id	AC3
Number of Residues	6
Details	binding site for residue PCW A 1003

Chain	Residue
A	LYS252
A	PHE256
A	GLN259
A	LYS824
A	LEU827
A	ILE828

site_id	AC4
Number of Residues	3
Details	binding site for residue PCW A 1004

Chain	Residue
A	GLY830
A	TRP831
A	LEU991

site_id	AC5
Number of Residues	2
Details	binding site for residue PCW A 1005

Chain	Residue
A	PHE985
A	ARG988

site_id	AC6
Number of Residues	1
Details	binding site for residue PCW A 1006

Chain	Residue
A	ARG324

site_id	AC7
Number of Residues	11
Details	binding site for residue MPD A 1007

Chain	Residue
A	THR499
A	PRO500
A	LYS502
A	PRO503
A	SER504
A	THR506
A	SER507
A	MET508
A	PRO662
A	ARG666
A	PHE689

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	ASP351-THR357

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	662
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	108
Details	Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	17
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	18
Details	Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	19
Details	Region: {"description":"Interaction with HAX1","evidences":[{"source":"PubMed","id":"18971376","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	31
Details	Region: {"description":"Interaction with PLN","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Active site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P11607","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O55143","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"PubMed","id":"16399855","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q64578","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)