Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KBC

Crystal structure of GltPh K55C-A364C mutant crosslinked with divalent mercury

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005283	molecular_function	amino acid:sodium symporter activity
A	0005886	cellular_component	plasma membrane
A	0006835	biological_process	dicarboxylic acid transport
A	0006865	biological_process	amino acid transport
A	0015108	molecular_function	chloride transmembrane transporter activity
A	0015183	molecular_function	L-aspartate transmembrane transporter activity
A	0015293	molecular_function	symporter activity
A	0015501	molecular_function	glutamate:sodium symporter activity
A	0016020	cellular_component	membrane
A	0022857	molecular_function	transmembrane transporter activity
A	0035725	biological_process	sodium ion transmembrane transport
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0046942	biological_process	carboxylic acid transport
A	0070207	biological_process	protein homotrimerization
A	0070778	biological_process	L-aspartate transmembrane transport
A	0140009	biological_process	L-aspartate import across plasma membrane
A	1902476	biological_process	chloride transmembrane transport
B	0005283	molecular_function	amino acid:sodium symporter activity
B	0005886	cellular_component	plasma membrane
B	0006835	biological_process	dicarboxylic acid transport
B	0006865	biological_process	amino acid transport
B	0015108	molecular_function	chloride transmembrane transporter activity
B	0015183	molecular_function	L-aspartate transmembrane transporter activity
B	0015293	molecular_function	symporter activity
B	0015501	molecular_function	glutamate:sodium symporter activity
B	0016020	cellular_component	membrane
B	0022857	molecular_function	transmembrane transporter activity
B	0035725	biological_process	sodium ion transmembrane transport
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0046942	biological_process	carboxylic acid transport
B	0070207	biological_process	protein homotrimerization
B	0070778	biological_process	L-aspartate transmembrane transport
B	0140009	biological_process	L-aspartate import across plasma membrane
B	1902476	biological_process	chloride transmembrane transport
C	0005283	molecular_function	amino acid:sodium symporter activity
C	0005886	cellular_component	plasma membrane
C	0006835	biological_process	dicarboxylic acid transport
C	0006865	biological_process	amino acid transport
C	0015108	molecular_function	chloride transmembrane transporter activity
C	0015183	molecular_function	L-aspartate transmembrane transporter activity
C	0015293	molecular_function	symporter activity
C	0015501	molecular_function	glutamate:sodium symporter activity
C	0016020	cellular_component	membrane
C	0022857	molecular_function	transmembrane transporter activity
C	0035725	biological_process	sodium ion transmembrane transport
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0046942	biological_process	carboxylic acid transport
C	0070207	biological_process	protein homotrimerization
C	0070778	biological_process	L-aspartate transmembrane transport
C	0140009	biological_process	L-aspartate import across plasma membrane
C	1902476	biological_process	chloride transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ASP A 500

Chain	Residue
A	ARG276
A	GLY359
A	ASP394
A	ARG397
A	THR398
A	ASN401
A	SER277
A	SER278
A	MET311
A	THR314
A	THR352
A	GLY354
A	VAL355
A	ALA358

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ASP B 500

Chain	Residue
B	ARG276
B	SER277
B	SER278
B	MET311
B	THR314
B	THR352
B	GLY354
B	VAL355
B	ALA358
B	GLY359
B	ASP394
B	ARG397
B	THR398
B	ASN401

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ASP C 500

Chain	Residue
C	ARG276
C	SER277
C	SER278
C	MET311
C	THR314
C	THR352
C	GLY354
C	VAL355
C	ALA358
C	GLY359
C	ASP394
C	ARG397
C	THR398
C	ASN401

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HG A 501

Chain	Residue
A	CYS55
A	CYS364
A	LEU374
A	TYR383

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 454

Chain	Residue
A	GLY306
A	ILE309
A	ASN310
A	ASN401
A	ASP405

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 453

Chain	Residue
A	THR308
A	MET311
A	SER349
A	ILE350
A	GLY351
A	THR352

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HG B 501

Chain	Residue
B	CYS55
B	CYS364
B	LEU374
B	TYR383

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 454

Chain	Residue
B	GLY306
B	ILE309
B	ASN310
B	ASN401
B	ASP405

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B 453

Chain	Residue
B	THR308
B	MET311
B	SER349
B	ILE350
B	GLY351
B	THR352

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HG C 501

Chain	Residue
C	CYS55
C	CYS364
C	LEU374
C	TYR383

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 454

Chain	Residue
C	GLY306
C	ILE309
C	ASN310
C	ASN401
C	ASP405

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA C 453

Chain	Residue
C	THR308
C	MET311
C	SER349
C	ILE350
C	GLY351
C	THR352

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	267
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:15483603

Chain	Residue	Details
A	LYS252-SER260
A	LYS290-GLY297
A	ALA413-ALA425
B	MET1-PRO11
B	PHE63-ARG80
B	LEU161-LYS196
B	LYS252-SER260
B	LYS290-GLY297
B	ALA413-ALA425
C	MET1-PRO11
C	PHE63-ARG80
C	LEU161-LYS196
C	LYS252-SER260
C	LYS290-GLY297
C	ALA413-ALA425
A	MET1-PRO11
A	PHE63-ARG80
A	LEU161-LYS196

site_id	SWS_FT_FI2
Number of Residues	54
Details	TRANSMEM: Helical; Name=1 => ECO:0000269\|PubMed:15483603

Chain	Residue	Details
B	VAL12-LEU30
C	VAL12-LEU30
A	VAL12-LEU30

site_id	SWS_FT_FI3
Number of Residues	216
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:15483603

Chain	Residue	Details
A	ALA321-GLN337
A	PRO373-ALA391
B	GLY31-THR41
B	ALA104-GLN121
B	GLU219-LYS230
B	ALA321-GLN337
B	PRO373-ALA391
C	GLY31-THR41
C	ALA104-GLN121
C	GLU219-LYS230
C	ALA321-GLN337
C	PRO373-ALA391
A	GLY31-THR41
A	ALA104-GLN121
A	GLU219-LYS230

site_id	SWS_FT_FI4
Number of Residues	60
Details	TRANSMEM: Helical; Name=2 => ECO:0000269\|PubMed:15483603

Chain	Residue	Details
B	TYR42-VAL62
C	TYR42-VAL62
A	TYR42-VAL62

site_id	SWS_FT_FI5
Number of Residues	66
Details	TRANSMEM: Helical; Name=3 => ECO:0000269\|PubMed:15483603

Chain	Residue	Details
B	VAL81-MET103
C	VAL81-MET103
A	VAL81-MET103

site_id	SWS_FT_FI6
Number of Residues	114
Details	TRANSMEM: Discontinuously helical; Name=4 => ECO:0000269\|PubMed:15483603

Chain	Residue	Details
B	PHE122-ILE160
C	PHE122-ILE160
A	PHE122-ILE160

site_id	SWS_FT_FI7
Number of Residues	63
Details	TRANSMEM: Helical; Name=5 => ECO:0000269\|PubMed:15483603

Chain	Residue	Details
B	ILE197-ALA218
C	ILE197-ALA218
A	ILE197-ALA218

site_id	SWS_FT_FI8
Number of Residues	60
Details	TRANSMEM: Helical; Name=6 => ECO:0000269\|PubMed:15483603

Chain	Residue	Details
A	VAL231-LEU251
B	VAL231-LEU251
C	VAL231-LEU251

site_id	SWS_FT_FI9
Number of Residues	186
Details	INTRAMEM: Discontinuously helical => ECO:0000269\|PubMed:15483603

Chain	Residue	Details
A	PHE261-ALA289
A	GLN338-LEU372
B	PHE261-ALA289
B	GLN338-LEU372
C	PHE261-ALA289
C	GLN338-LEU372

site_id	SWS_FT_FI10
Number of Residues	66
Details	TRANSMEM: Discontinuously helical; Name=7 => ECO:0000269\|PubMed:15483603

Chain	Residue	Details
A	ILE298-VAL320
B	ILE298-VAL320
C	ILE298-VAL320

site_id	SWS_FT_FI11
Number of Residues	60
Details	TRANSMEM: Helical; Name=8 => ECO:0000269\|PubMed:15483603

Chain	Residue	Details
A	ILE392-VAL412
B	ILE392-VAL412
C	ILE392-VAL412

site_id	SWS_FT_FI12
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:17230192, ECO:0007744\|PDB:2NWL, ECO:0007744\|PDB:2NWX, ECO:0007744\|PDB:3KBC

Chain	Residue	Details
B	VAL355
B	ASP394
C	ARG276
C	THR314
C	VAL355
C	ASP394
A	ARG276
A	THR314
A	VAL355
A	ASP394
B	ARG276
B	THR314

site_id	SWS_FT_FI13
Number of Residues	15
Details	BINDING: BINDING => ECO:0000305\|PubMed:17230192, ECO:0007744\|PDB:2NWX

Chain	Residue	Details
B	THR308
B	THR352
B	ASN401
B	ASP405
C	GLY306
C	THR308
C	THR352
C	ASN401
C	ASP405
A	GLY306
A	THR308
A	THR352
A	ASN401
A	ASP405
B	GLY306

site_id	SWS_FT_FI14
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305\|PubMed:17230192, ECO:0007744\|PDB:2NWX, ECO:0007744\|PDB:4X2S

Chain	Residue	Details
A	ASN310
B	ASN310
C	ASN310

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