Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2H0K

Crystal Structure of a Mutant of Rat Annexin A5

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001786	molecular_function	phosphatidylserine binding
A	0005388	molecular_function	P-type calcium transporter activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005544	molecular_function	calcium-dependent phospholipid binding
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0007596	biological_process	blood coagulation
A	0007599	biological_process	hemostasis
A	0008021	cellular_component	synaptic vesicle
A	0009897	cellular_component	external side of plasma membrane
A	0012506	cellular_component	vesicle membrane
A	0014704	cellular_component	intercalated disc
A	0017046	molecular_function	peptide hormone binding
A	0030018	cellular_component	Z disc
A	0030195	biological_process	negative regulation of blood coagulation
A	0030425	cellular_component	dendrite
A	0030672	cellular_component	synaptic vesicle membrane
A	0030971	molecular_function	receptor tyrosine kinase binding
A	0042383	cellular_component	sarcolemma
A	0042802	molecular_function	identical protein binding
A	0042995	cellular_component	cell projection
A	0043025	cellular_component	neuronal cell body
A	0043065	biological_process	positive regulation of apoptotic process
A	0043204	cellular_component	perikaryon
A	0043679	cellular_component	axon terminus
A	0050819	biological_process	negative regulation of coagulation
A	0051592	biological_process	response to calcium ion
A	0070588	biological_process	calcium ion transmembrane transport
A	0071284	biological_process	cellular response to lead ion
A	0072563	cellular_component	endothelial microparticle
A	0097066	biological_process	response to thyroid hormone
A	0097211	biological_process	cellular response to gonadotropin-releasing hormone
A	1901317	biological_process	regulation of flagellated sperm motility
A	1902721	biological_process	negative regulation of prolactin secretion
B	0001786	molecular_function	phosphatidylserine binding
B	0005388	molecular_function	P-type calcium transporter activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005544	molecular_function	calcium-dependent phospholipid binding
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0007596	biological_process	blood coagulation
B	0007599	biological_process	hemostasis
B	0008021	cellular_component	synaptic vesicle
B	0009897	cellular_component	external side of plasma membrane
B	0012506	cellular_component	vesicle membrane
B	0014704	cellular_component	intercalated disc
B	0017046	molecular_function	peptide hormone binding
B	0030018	cellular_component	Z disc
B	0030195	biological_process	negative regulation of blood coagulation
B	0030425	cellular_component	dendrite
B	0030672	cellular_component	synaptic vesicle membrane
B	0030971	molecular_function	receptor tyrosine kinase binding
B	0042383	cellular_component	sarcolemma
B	0042802	molecular_function	identical protein binding
B	0042995	cellular_component	cell projection
B	0043025	cellular_component	neuronal cell body
B	0043065	biological_process	positive regulation of apoptotic process
B	0043204	cellular_component	perikaryon
B	0043679	cellular_component	axon terminus
B	0050819	biological_process	negative regulation of coagulation
B	0051592	biological_process	response to calcium ion
B	0070588	biological_process	calcium ion transmembrane transport
B	0071284	biological_process	cellular response to lead ion
B	0072563	cellular_component	endothelial microparticle
B	0097066	biological_process	response to thyroid hormone
B	0097211	biological_process	cellular response to gonadotropin-releasing hormone
B	1901317	biological_process	regulation of flagellated sperm motility
B	1902721	biological_process	negative regulation of prolactin secretion

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 401

Chain	Residue
A	MET26
A	GLY28
A	GLY30
A	GLU70

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 402

Chain	Residue
A	LYS68
A	LEU71
A	GLU76
A	HOH477

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA A 403

Chain	Residue
A	GLU33
A	THR31

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 404

Chain	Residue
A	LEU98
A	GLY100
A	ALA101
A	THR103
A	ASP142

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA A 412

Chain	Residue
A	THR187
A	GLU226

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA A 406

Chain	Residue
A	THR103
A	GLU105

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 402

Chain	Residue
B	LYS68
B	LEU71
B	GLU76
B	HOH451

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA B 403

Chain	Residue
A	ASP34
B	THR31
B	GLU33

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 404

Chain	Residue
B	LEU98
B	GLY100
B	ALA101
B	THR103
B	ASP142

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA B 412

Chain	Residue
B	THR187
B	GLU226

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA B 406

Chain	Residue
B	THR103
B	GLU105

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA A 409

Chain	Residue
A	THR187
A	GLU189
A	HOH415

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 410

Chain	Residue
A	MET257
A	GLY259
A	GLY261
A	ASP301
A	HOH416

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 408

Chain	Residue
A	ASP224
A	THR227
A	GLU232
A	HOH417

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 407

Chain	Residue
A	GLY181
A	LYS184
A	GLY186
A	GLU226
A	HOH418

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 414

Chain	Residue
A	GLU93
A	HIS96
A	HIS265
A	HOH419

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 401

Chain	Residue
B	MET26
B	GLY28
B	GLY30
B	GLU70
B	HOH415

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA B 409

Chain	Residue
B	THR187
B	GLU189
B	HOH416

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 410

Chain	Residue
B	MET257
B	GLY259
B	GLY261
B	ASP301
B	HOH417
B	HOH464

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 408

Chain	Residue
B	ASP224
B	THR227
B	GLU232
B	HOH418

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 407

Chain	Residue
B	GLY181
B	LYS184
B	GLY186
B	GLU226
B	HOH419

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 414

Chain	Residue
B	GLU93
B	HIS96
B	HIS265
B	HOH420

Functional Information from PROSITE/UniProt

site_id	PS00223
Number of Residues	53
Details	ANNEXIN_1 Annexin repeat signature. GTdedsilnlLtaRsnaQrqQiaeeFetlfgrdLvndMkseltGkfeklIvaL

Chain	Residue	Details
A	GLY30-LEU82
A	GLY102-LEU154
A	GLY186-VAL238
A	GLY261-LEU313

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	142
Details	Repeat: {"description":"Annexin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	142
Details	Repeat: {"description":"Annexin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	144
Details	Repeat: {"description":"Annexin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	142
Details	Repeat: {"description":"Annexin 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Motif: {"description":"[IL]-x-C-x-x-[DE] motif","evidences":[{"source":"UniProtKB","id":"P08758","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"7583670","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	10
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P08758","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P48036","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P08758","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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