5MPM

SERCA2a from pig heart

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000045	biological_process	autophagosome assembly
A	0000166	molecular_function	nucleotide binding
A	0005215	molecular_function	transporter activity
A	0005388	molecular_function	P-type calcium transporter activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0006816	biological_process	calcium ion transport
A	0006874	biological_process	intracellular calcium ion homeostasis
A	0010882	biological_process	regulation of cardiac muscle contraction by calcium ion signaling
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	0033017	cellular_component	sarcoplasmic reticulum membrane
A	0046872	molecular_function	metal ion binding
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	0140056	biological_process	organelle localization by membrane tethering
A	1990456	biological_process	mitochondrion-endoplasmic reticulum membrane tethering

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue MGF A 1001

Chain	Residue
A	GLY182
A	HOH1101
A	HOH1104
A	ASP351
A	LYS352
A	THR353
A	THR624
A	GLY625
A	LYS683
A	ASN705
A	MG1004

---

site_id	AC2
Number of Residues	15
Details	binding site for residue CZA A 1002

Chain	Residue
A	GLN56
A	PHE57
A	ASP59
A	LEU61
A	VAL62
A	LEU65
A	LEU98
A	ASN101
A	ALA102
A	LEU253
A	ILE307
A	PRO308
A	MG1003
A	HOH1102
A	HOH1103

---

site_id	AC3
Number of Residues	4
Details	binding site for residue MG A 1003

Chain	Residue
A	GLN56
A	CZA1002
A	HOH1102
A	HOH1103

---

site_id	AC4
Number of Residues	7
Details	binding site for residue MG A 1004

Chain	Residue
A	GLY182
A	ASP351
A	THR353
A	ASP702
A	MGF1001
A	HOH1104
A	HOH1105

---

site_id	AC5
Number of Residues	4
Details	binding site for residue K A 1005

Chain	Residue
A	LEU710
A	LYS711
A	SER713
A	GLU731

---

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	TOPO_DOM: Cytoplasmic => ECO:0000305

Chain	Residue	Details
A	MET1-THR48
A	ASN111-LEU253
A	VAL314-MET756
A	PHE808-LEU827
A	GLU917-ASN929

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	TRANSMEM: Helical; Name=1 => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	LEU49-ALA69

---

site_id	SWS_FT_FI3
Number of Residues	108
Details	TOPO_DOM: Lumenal => ECO:0000305

Chain	Residue	Details
A	CYS70-VAL89
A	ILE274-TYR295
A	THR777-LEU786
A	ALA851-MET896
A	VAL949-LEU963

---

site_id	SWS_FT_FI4
Number of Residues	20
Details	TRANSMEM: Helical; Name=2 => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	GLU90-ARG110

---

site_id	SWS_FT_FI5
Number of Residues	19
Details	TRANSMEM: Helical; Name=3 => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	ASP254-ILE273

---

site_id	SWS_FT_FI6
Number of Residues	17
Details	TRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	PHE296-ALA313

---

site_id	SWS_FT_FI7
Number of Residues	19
Details	TRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	LYS757-LEU776

---

site_id	SWS_FT_FI8
Number of Residues	20
Details	TRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	ILE787-GLY807

---

site_id	SWS_FT_FI9
Number of Residues	22
Details	TRANSMEM: Helical; Name=7 => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	ILE828-ALA850

---

site_id	SWS_FT_FI10
Number of Residues	19
Details	TRANSMEM: Helical; Name=8 => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	THR897-SER916

---

site_id	SWS_FT_FI11
Number of Residues	18
Details	TRANSMEM: Helical; Name=9 => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	ILE930-TYR948

---

site_id	SWS_FT_FI12
Number of Residues	20
Details	TRANSMEM: Helical; Name=10 => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	THR964-LYS984

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	ACT_SITE: 4-aspartylphosphate intermediate => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	ASP351

---

site_id	SWS_FT_FI14
Number of Residues	15
Details	BINDING: BINDING => ECO:0000305|PubMed:30777856, ECO:0007744|PDB:6HXB

Chain	Residue	Details
A	VAL304
A	ASN705
A	ASN767
A	GLU770
A	ASN795
A	THR798
A	ASP799
A	ALA305
A	ILE307
A	GLU309
A	GLU442
A	ARG489
A	LYS514
A	ASP626
A	ARG677

---

site_id	SWS_FT_FI15
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:30777856, ECO:0007744|PDB:5MPM

Chain	Residue	Details
A	ASP351
A	THR353
A	ASP702

---

site_id	SWS_FT_FI16
Number of Residues	5
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P04191

Chain	Residue	Details
A	ARG559
A	THR624
A	GLY625
A	LYS683
A	GLU907

---

site_id	SWS_FT_FI17
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O55143

Chain	Residue	Details
A	SER38
A	SER531

---

site_id	SWS_FT_FI18
Number of Residues	2
Details	MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P16615

Chain	Residue	Details
A	TYR294
A	TYR295

---

site_id	SWS_FT_FI19
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q64578

Chain	Residue	Details
A	THR441

---

site_id	SWS_FT_FI20
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P16615

Chain	Residue	Details
A	SER580
A	SER663

---