Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5LVS

Self-assembled protein-aromatic foldamer complexes with 2:3 and 2:2:1 stoichiometries

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004064	molecular_function	arylesterase activity
A	0004089	molecular_function	carbonate dehydratase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0008270	molecular_function	zinc ion binding
A	0015670	biological_process	carbon dioxide transport
A	0016829	molecular_function	lyase activity
A	0018820	molecular_function	cyanamide hydratase activity
A	0038166	biological_process	angiotensin-activated signaling pathway
A	0044070	biological_process	regulation of monoatomic anion transport
A	0045177	cellular_component	apical part of cell
A	0046872	molecular_function	metal ion binding
A	0051453	biological_process	regulation of intracellular pH
A	0070062	cellular_component	extracellular exosome
A	2001150	biological_process	positive regulation of dipeptide transmembrane transport
B	0004064	molecular_function	arylesterase activity
B	0004089	molecular_function	carbonate dehydratase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0008270	molecular_function	zinc ion binding
B	0015670	biological_process	carbon dioxide transport
B	0016829	molecular_function	lyase activity
B	0018820	molecular_function	cyanamide hydratase activity
B	0038166	biological_process	angiotensin-activated signaling pathway
B	0044070	biological_process	regulation of monoatomic anion transport
B	0045177	cellular_component	apical part of cell
B	0046872	molecular_function	metal ion binding
B	0051453	biological_process	regulation of intracellular pH
B	0070062	cellular_component	extracellular exosome
B	2001150	biological_process	positive regulation of dipeptide transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue ZN A 301

Chain	Residue
A	HIS94
A	HIS96
A	HIS119

site_id	AC2
Number of Residues	8
Details	binding site for residue GOL A 302

Chain	Residue
A	HOH436
A	HOH560
A	TRP5
A	PHE20
A	PRO200
A	PRO201
C	QUK304
H	QUJ301

site_id	AC3
Number of Residues	10
Details	binding site for residue GOL A 303

Chain	Residue
A	ASN62
A	HIS64
A	ALA65
A	ASN67
A	GLN92
A	HIS94
A	THR199
A	HOH460
A	HOH495
A	HOH510

site_id	AC4
Number of Residues	6
Details	binding site for residue GOL A 304

Chain	Residue
A	TYR7
A	PRO13
A	ASP242
A	TRP244
A	HOH412
A	HOH413

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL D 401

Chain	Residue
A	ASN67
A	GLN92
A	PHE130
D	QUJ303
A	HOH408

site_id	AC6
Number of Residues	6
Details	binding site for residue GOL A 305

Chain	Residue
A	THR35
A	ALA38
A	TRP191
A	PHE259
A	LYS260
A	HOH566

site_id	AC7
Number of Residues	3
Details	binding site for residue ZN B 301

Chain	Residue
B	HIS94
B	HIS96
B	HIS119

site_id	AC9
Number of Residues	5
Details	binding site for residue GOL B 302

Chain	Residue
B	TRP5
B	PRO200
B	PRO201
H	QUK303
B	HOH441

site_id	AD1
Number of Residues	9
Details	binding site for residue GOL B 303

Chain	Residue
B	ASN62
B	ALA65
B	ASN67
B	GLN92
B	HIS94
B	THR199
B	HOH471
B	HOH488
B	HOH535

site_id	AD2
Number of Residues	6
Details	binding site for residue GOL B 304

Chain	Residue
B	TYR7
B	PRO13
B	ASP242
B	TRP244
B	HOH403
B	HOH408

site_id	AD3
Number of Residues	8
Details	binding site for residue GOL B 305

Chain	Residue
A	ASN177
B	LYS167
B	ASN229
B	ASN231
B	GLY232
B	GLU233
B	GLY234
B	GLU235

site_id	AD4
Number of Residues	4
Details	binding site for residue GOL B 306

Chain	Residue
B	ASN67
B	GLN92
B	PHE130
B	HOH404

site_id	AD5
Number of Residues	8
Details	binding site for residue GOL B 307

Chain	Residue
B	TYR51
B	ASP52
B	ALA54
B	LYS126
B	ASN177
B	ASP179
B	ARG181
B	HOH511

site_id	AD6
Number of Residues	6
Details	binding site for residue GOL B 308

Chain	Residue
B	THR35
B	ALA38
B	TRP191
B	PHE259
B	LYS260
B	HOH507

site_id	AD8
Number of Residues	11
Details	binding site for residues QUK A 303 and QVS A 304

Chain	Residue
A	HIS3
A	ASP19
A	PHE20
C	QVE306
A	GOL302
C	HOH405
C	HOH406
B	ASP129
B	LYS132
C	QUJ303
A	HOH401

site_id	AD9
Number of Residues	30
Details	binding site for residues QUK A 303 and QUJ B 301

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
C	QVS305
C	QVE306
A	GOL302
D	QUJ303
A	HOH403
C	HOH405
B	HIS94
B	HIS96
B	HIS119
B	PHE130
B	GLY131
B	LEU197
B	THR198
B	THR199
B	PRO201
B	TRP208
B	ZN301
D	QUK304
D	QVS305
B	GOL302
B	GOL303
B	GOL306
A	HOH401
H	QUK303
B	HOH426
D	HOH503
A	HIS3

site_id	AE1
Number of Residues	11
Details	binding site for residues QVS A 304 and QVE A 305

Chain	Residue
A	SER2
A	HIS3
A	ASP19
A	PHE20
C	QUK304
C	HOH402
C	HOH403
C	HOH406
B	ASP129
B	LYS132
C	QUJ303

site_id	AE2
Number of Residues	21
Details	binding site for residues QUJ A 311 and QUK B 304

Chain	Residue
A	HIS3
A	ASP19
A	PHE20
A	GLY131
C	QUK304
C	QVE306
D	GOL401
H	QUJ301
C	HOH406
B	HIS3
B	ASN67
B	GLN92
B	ASP129
B	PHE130
B	LYS132
C	QUJ303
D	QVS305
D	QVE306
H	QUK303
B	HOH404
D	HOH504

site_id	AE3
Number of Residues	13
Details	binding site for residues FOR A 312 and QUK B 315

Chain	Residue
D	QUJ303
H	QUJ301
B	TYR51
B	ASP52
B	ALA54
B	LYS126
B	ASN177
B	ASP179
B	ARG181
D	QUK304
B	GOL302
A	HOH401
B	HOH511

site_id	AE4
Number of Residues	6
Details	binding site for residues FOR A 312 and QUK A 313

Chain	Residue
C	QUK304
A	GOL302
H	QUJ301
C	QUJ303
A	HOH401
H	QUK303

site_id	AE5
Number of Residues	18
Details	binding site for residues QUK A 313 and QUJ B 314

Chain	Residue
C	QUK304
A	GOL302
D	QUJ303
A	HOH436
H	HOH406
H	HOH404
B	THR35
B	ALA38
B	TRP191
B	PHE259
B	LYS260
C	QUJ303
D	QUK304
H	QUK303
H	HOH402
B	HOH507
H	HOH403
H	HOH405

site_id	AE6
Number of Residues	12
Details	binding site for residues QUJ A 314 and QUK B 315

Chain	Residue
C	QUK304
A	GOL302
D	QUJ303
A	HOH436
H	HOH406
H	HOH404
C	QUJ303
D	QUK304
B	GOL302
H	HOH402
H	HOH403
H	HOH405

site_id	AE7
Number of Residues	10
Details	binding site for residues QUK B 304 and QVS B 305

Chain	Residue
A	ASP129
A	LYS132
D	QUJ303
H	QUJ301
A	HOH561
B	HIS3
B	ASP19
D	QVE306
H	QUK303
D	HOH504

site_id	AE8
Number of Residues	9
Details	binding site for residues QVS B 305 and QVE B 306

Chain	Residue
A	ASP129
A	LYS132
D	QUJ303
A	HOH561
B	HIS3
B	ASP19
D	QUK304
D	HOH502
D	HOH505

Functional Information from PROSITE/UniProt

site_id	PS00162
Number of Residues	17
Details	ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV

Chain	Residue	Details
A	SER105-VAL121

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	512
Details	Domain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15667203","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11076507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12499545","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1336460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1433293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1909891","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19583303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151020","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4621826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7803386","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7901850","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8218160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8262987","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8399159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8431430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8451242","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8482389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8639494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8987974","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9865942","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11076507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12499545","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1336460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1433293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1909891","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19583303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151020","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7803386","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7901850","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8218160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8262987","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8399159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8431430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8451242","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8482389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8639494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8987974","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9865942","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10550681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19520834","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Site: {"description":"Fine-tunes the proton-transfer properties of H-64","evidences":[{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Site: {"description":"Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine","evidences":[{"source":"PubMed","id":"16214338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9265618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Site: {"description":"Involved in the binding of some activators, including histamine and L-histidine","evidences":[{"source":"PubMed","id":"16214338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9265618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P27139","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 216

Chain	Residue	Details
A	HIS64	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS94	metal ligand
A	HIS96	metal ligand
A	GLU106	activator, electrostatic stabiliser, hydrogen bond acceptor
A	HIS119	metal ligand
A	THR198	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

site_id	MCSA2
Number of Residues	6
Details	M-CSA 216

Chain	Residue	Details
B	HIS64	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS94	metal ligand
B	HIS96	metal ligand
B	GLU106	activator, electrostatic stabiliser, hydrogen bond acceptor
B	HIS119	metal ligand
B	THR198	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

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