Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5L70

CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH A QUINOLINE OLIGOAMIDE FOLDAMER

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002009	biological_process	morphogenesis of an epithelium
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	0016020	cellular_component	membrane
A	0016829	molecular_function	lyase activity
A	0018820	molecular_function	cyanamide hydratase activity
A	0032230	biological_process	positive regulation of synaptic transmission, GABAergic
A	0032849	biological_process	positive regulation of cellular pH reduction
A	0038166	biological_process	angiotensin-activated signaling pathway
A	0043209	cellular_component	myelin sheath
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	0046903	biological_process	secretion
A	0051453	biological_process	regulation of intracellular pH
A	0070050	biological_process	neuron cellular homeostasis
A	0070062	cellular_component	extracellular exosome
A	2001150	biological_process	positive regulation of dipeptide transmembrane transport
A	2001225	biological_process	regulation of chloride transport
B	0002009	biological_process	morphogenesis of an epithelium
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	0016020	cellular_component	membrane
B	0016829	molecular_function	lyase activity
B	0018820	molecular_function	cyanamide hydratase activity
B	0032230	biological_process	positive regulation of synaptic transmission, GABAergic
B	0032849	biological_process	positive regulation of cellular pH reduction
B	0038166	biological_process	angiotensin-activated signaling pathway
B	0043209	cellular_component	myelin sheath
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	0046903	biological_process	secretion
B	0051453	biological_process	regulation of intracellular pH
B	0070050	biological_process	neuron cellular homeostasis
B	0070062	cellular_component	extracellular exosome
B	2001150	biological_process	positive regulation of dipeptide transmembrane transport
B	2001225	biological_process	regulation of chloride 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	5
Details	binding site for residue ZN A 302

Chain	Residue
A	HIS4
A	HIS64
D	QVS304
D	QVE306
A	HOH431

site_id	AC3
Number of Residues	9
Details	binding site for residue GOL A 303

Chain	Residue
A	ASN62
A	HIS64
A	THR199
A	PRO200
D	QVE306
A	HOH451
A	HOH513
A	HOH539
A	TRP5

site_id	AC4
Number of Residues	2
Details	binding site for residue ZN A 304

Chain	Residue
A	HIS17
A	HOH430

site_id	AC5
Number of Residues	5
Details	binding site for residue ZN A 305

Chain	Residue
A	HIS36
A	ZN309
B	ASP34
B	HOH462
B	HOH500

site_id	AC6
Number of Residues	5
Details	binding site for residue ZN A 306

Chain	Residue
A	ASP34
A	ZN309
A	HOH536
B	HIS36
B	HOH495

site_id	AC7
Number of Residues	3
Details	binding site for residue ZN A 307

Chain	Residue
A	ASP174
A	HOH506
B	GLU233

site_id	AC8
Number of Residues	1
Details	binding site for residue ZN A 308

Chain	Residue
A	GLU238

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN A 309

Chain	Residue
A	ZN305
A	ZN306
A	HOH536
B	HOH500

site_id	AD1
Number of Residues	4
Details	binding site for residue ZN A 310

Chain	Residue
A	ASP72
A	HOH544
A	HOH563
A	HOH582

site_id	AD2
Number of Residues	6
Details	binding site for residue GOL A 311

Chain	Residue
A	THR35
A	ALA38
A	TRP191
A	PHE259
A	LYS260
A	HOH414

site_id	AD3
Number of Residues	3
Details	binding site for residue ZN B 301

Chain	Residue
B	HIS94
B	HIS96
B	HIS119

site_id	AD4
Number of Residues	5
Details	binding site for residue ZN B 302

Chain	Residue
C	QVS304
C	QVE306
C	HOH401
B	HIS4
B	HIS64

site_id	AD5
Number of Residues	7
Details	binding site for residue GOL B 303

Chain	Residue
C	QVE306
B	TRP5
B	ASN62
B	THR199
B	PRO200
B	PRO201
B	HOH437

site_id	AD6
Number of Residues	2
Details	binding site for residue ZN B 304

Chain	Residue
B	HIS17
B	HOH438

site_id	AD7
Number of Residues	3
Details	binding site for residue ZN B 305

Chain	Residue
B	ASP72
B	HOH411
B	HOH510

site_id	AD8
Number of Residues	5
Details	binding site for residue GOL B 306

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

site_id	AE1
Number of Residues	11
Details	binding site for residues QVS A 305 and QUK A 306

Chain	Residue
A	HIS4
A	ASP19
A	PHE20
A	ZN302
D	QVE306
C	QOL303
C	QVS304
A	HOH431
D	HOH402
D	HOH404
D	QOL303

site_id	AE2
Number of Residues	19
Details	binding site for residues QVS A 305 and QOL B 301

Chain	Residue
B	PRO201
B	HOH437
D	HOH405
A	HIS4
A	HIS94
A	HIS96
A	HIS119
A	ZN302
D	QUK305
D	QVE306
C	QOL303
C	QVS304
C	QVE306
A	HOH431
D	HOH404
B	TRP5
B	ASN62
B	THR199
B	PRO200

site_id	AE3
Number of Residues	13
Details	binding site for residues QUK A 306 and QVE A 307

Chain	Residue
A	HIS4
A	TRP5
A	ASP19
A	PHE20
A	HIS64
A	ZN302
A	GOL303
D	QVS304
D	HOH401
A	HOH431
D	HOH402
D	HOH406
D	QOL303

site_id	AE4
Number of Residues	8
Details	binding site for residues QOL A 316 and QVS A 317

Chain	Residue
D	QVS304
C	QUK305
C	QVE306
C	HOH401
C	HOH404
B	HIS4
D	QOL303
B	ZN302

site_id	AE5
Number of Residues	9
Details	binding site for residues QVS A 317 and QUK A 318

Chain	Residue
D	QVS304
C	QOL303
C	QVE306
C	HOH401
B	HIS4
B	ASP19
B	PHE20
D	QOL303
B	ZN302

site_id	AE6
Number of Residues	12
Details	binding site for residues QUK A 318 and QVE A 319

Chain	Residue
C	QOL303
C	QVS304
C	HOH401
C	HOH403
C	HOH404
B	HIS4
B	TRP5
B	ASP19
B	PHE20
B	HIS64
B	ZN302
B	GOL303

site_id	AE7
Number of Residues	21
Details	binding site for residues QOL B 301 and 6H0 B 303

Chain	Residue
D	QVS304
D	QUK305
D	QVE306
C	QOL303
C	QVS304
C	QVE306
B	HIS94
B	HIS96
B	HIS119
B	VAL121
B	PHE130
B	VAL142
B	LEU197
B	THR198
B	THR199
B	PRO201
B	TRP208
B	ZN301
B	GOL303
D	HOH403
D	HOH405

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	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)