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	0035725	biological_process	sodium ion transmembrane transport
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
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	0035725	biological_process	sodium ion transmembrane transport
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
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	0035725	biological_process	sodium ion transmembrane transport
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
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	54
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	216
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	60
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	201
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	66
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	114
Details	Transmembrane: {"description":"Discontinuously helical; Name=4","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	63
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	60
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	186
Details	Intramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	66
Details	Transmembrane: {"description":"Discontinuously helical; Name=7","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	60
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17230192","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NWL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NWX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KBC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17230192","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2NWX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17230192","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2NWX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X2S","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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