Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5L9E

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	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
C	0004064	molecular_function	arylesterase activity
C	0004089	molecular_function	carbonate dehydratase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0008270	molecular_function	zinc ion binding
C	0015670	biological_process	carbon dioxide transport
C	0016829	molecular_function	lyase activity
C	0018820	molecular_function	cyanamide hydratase activity
C	0038166	biological_process	angiotensin-activated signaling pathway
C	0044070	biological_process	regulation of monoatomic anion transport
C	0045177	cellular_component	apical part of cell
C	0046872	molecular_function	metal ion binding
C	0051453	biological_process	regulation of intracellular pH
C	0070062	cellular_component	extracellular exosome
C	2001150	biological_process	positive regulation of dipeptide transmembrane transport
D	0004064	molecular_function	arylesterase activity
D	0004089	molecular_function	carbonate dehydratase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0008270	molecular_function	zinc ion binding
D	0015670	biological_process	carbon dioxide transport
D	0016829	molecular_function	lyase activity
D	0018820	molecular_function	cyanamide hydratase activity
D	0038166	biological_process	angiotensin-activated signaling pathway
D	0044070	biological_process	regulation of monoatomic anion transport
D	0045177	cellular_component	apical part of cell
D	0046872	molecular_function	metal ion binding
D	0051453	biological_process	regulation of intracellular pH
D	0070062	cellular_component	extracellular exosome
D	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	4
Details	binding site for residue ZN A 302

Chain	Residue
A	HIS4
A	HIS64
E	QVE304
E	QVE306

site_id	AC3
Number of Residues	2
Details	binding site for residue ZN A 303

Chain	Residue
A	HIS17
C	GLU26

site_id	AC4
Number of Residues	3
Details	binding site for residue ZN A 304

Chain	Residue
A	ASP174
A	HOH441
C	HOH428

site_id	AC5
Number of Residues	3
Details	binding site for residue ZN A 305

Chain	Residue
A	ASP34
A	HIS36
A	HOH401

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN A 306

Chain	Residue
A	GLU186
A	HOH404
A	HOH431
B	ASP189

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN A 307

Chain	Residue
A	ASP52
A	HOH424
B	ASP52
B	HOH417

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

Chain	Residue
A	HIS15

site_id	AC9
Number of Residues	5
Details	binding site for residue GOL A 309

Chain	Residue
A	ASN62
A	ALA65
A	ASN67
A	GLN92
A	HOH406

site_id	AD1
Number of Residues	3
Details	binding site for residue ZN A 310

Chain	Residue
A	ASP189
A	LYS260
B	GLU186

site_id	AD2
Number of Residues	5
Details	binding site for residue ZN A 311

Chain	Residue
A	GLU233
A	GLU233
C	LYS171
C	GLU233
C	GLU233

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	4
Details	binding site for residue ZN B 302

Chain	Residue
B	HIS4
B	HIS64
F	QVE304
F	QVE306

site_id	AD5
Number of Residues	3
Details	binding site for residue ZN B 303

Chain	Residue
B	HIS17
B	LYS18
D	GLU26

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

Chain	Residue
B	ASP174
B	HOH425

site_id	AD7
Number of Residues	4
Details	binding site for residue ZN B 305

Chain	Residue
B	ASP34
B	HIS36
B	HOH401
B	HOH422

site_id	AD8
Number of Residues	4
Details	binding site for residue GOL B 306

Chain	Residue
B	ASN62
B	ALA65
B	ASN67
B	GLN92

site_id	AD9
Number of Residues	3
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS94
C	HIS96
C	HIS119

site_id	AE1
Number of Residues	5
Details	binding site for residue ZN C 302

Chain	Residue
C	HIS4
C	HIS64
G	QVE304
G	QVE306
C	HOH401

site_id	AE2
Number of Residues	4
Details	binding site for residue ZN C 303

Chain	Residue
A	GLU26
A	HOH413
A	HOH417
C	HIS17

site_id	AE3
Number of Residues	2
Details	binding site for residue ZN C 304

Chain	Residue
C	ASP174
C	HOH427

site_id	AE4
Number of Residues	4
Details	binding site for residue ZN C 305

Chain	Residue
B	GLU14
C	ASP34
C	HIS36
C	HOH413

site_id	AE5
Number of Residues	4
Details	binding site for residue GOL C 306

Chain	Residue
C	ASN62
C	ASN67
C	HIS94
C	THR199

site_id	AE6
Number of Residues	3
Details	binding site for residue ZN C 307

Chain	Residue
B	HIS10
C	HIS36
C	HOH403

site_id	AE7
Number of Residues	3
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS94
D	HIS96
D	HIS119

site_id	AE8
Number of Residues	4
Details	binding site for residue ZN D 302

Chain	Residue
D	HIS4
D	HIS64
H	QVE304
H	QVE306

site_id	AE9
Number of Residues	4
Details	binding site for residue ZN D 303

Chain	Residue
B	GLU26
B	HOH414
D	HIS17
D	HOH402

site_id	AF1
Number of Residues	2
Details	binding site for residue ZN D 304

Chain	Residue
B	HOH426
D	ASP174

site_id	AF2
Number of Residues	3
Details	binding site for residue ZN D 305

Chain	Residue
D	ASP34
D	HIS36
D	HOH425

site_id	AF3
Number of Residues	4
Details	binding site for residue GOL D 306

Chain	Residue
D	ALA65
D	ASN67
D	GLN92
D	ASN62

site_id	AF4
Number of Residues	4
Details	binding site for residue ZN D 307

Chain	Residue
B	GLU233
B	GLU233
D	GLU233
D	GLU233

site_id	AF6
Number of Residues	5
Details	binding site for residues QUJ A 303 and QVE A 304

Chain	Residue
A	HIS4
A	LYS169
E	QUJ305
E	QVE306
A	ZN302

site_id	AF7
Number of Residues	9
Details	binding site for residues QVE A 304 and QUJ A 305

Chain	Residue
A	HIS4
A	ASP19
A	PHE20
A	LYS169
A	PRO201
E	QUJ303
E	QVE306
A	ZN302
E	HOH401

site_id	AF8
Number of Residues	10
Details	binding site for residues QUJ A 305 and QVE A 306

Chain	Residue
A	HIS4
A	TRP5
A	ASP19
A	PHE20
A	HIS64
A	PRO201
E	QUJ303
E	QVE304
A	ZN302
E	HOH401

site_id	AG1
Number of Residues	4
Details	binding site for residues QUJ B 303 and QVE B 304

Chain	Residue
B	HIS4
F	QUJ305
F	QVE306
B	ZN302

site_id	AG2
Number of Residues	7
Details	binding site for residues QVE B 304 and QUJ B 305

Chain	Residue
B	HIS4
B	ASP19
B	PHE20
F	QUJ303
F	QVE306
B	ZN302
F	HOH401

site_id	AG3
Number of Residues	10
Details	binding site for residues QUJ B 305 and QVE B 306

Chain	Residue
B	HIS4
B	TRP5
B	ASP19
B	PHE20
B	HIS64
B	PRO201
F	QUJ303
F	QVE304
B	ZN302
F	HOH401

site_id	AG4
Number of Residues	13
Details	binding site for residues QUJ B 312 and QVE D 304

Chain	Residue
B	HIS4
F	QUJ303
F	QUJ305
F	QVE306
B	ZN302
D	HIS4
D	ASP19
D	PHE20
D	LYS169
H	QUJ303
H	QUJ303
H	QVE306
D	ZN302

site_id	AG5
Number of Residues	14
Details	binding site for residues QUJ B 312 and QVE D 305

Chain	Residue
B	ASP19
B	PHE20
F	QUJ303
F	QVE304
F	QVE306
F	HOH401
D	HIS4
D	TRP5
D	ASP19
D	PHE20
D	HIS64
H	QUJ303
H	QVE304
D	ZN302

site_id	AG7
Number of Residues	6
Details	binding site for residues QUJ C 303 and QVE C 304

Chain	Residue
C	HIS4
C	LYS169
G	QUJ305
G	QVE306
C	ZN302
C	HOH401

site_id	AG8
Number of Residues	8
Details	binding site for residues QVE C 304 and QUJ C 305

Chain	Residue
C	HIS4
C	ASP19
C	PHE20
C	LYS169
G	QUJ303
G	QVE306
C	ZN302
C	HOH401

site_id	AG9
Number of Residues	8
Details	binding site for residues QUJ C 305 and QVE C 306

Chain	Residue
C	HIS4
C	TRP5
C	ASP19
C	PHE20
C	HIS64
G	QUJ303
G	QVE304
C	ZN302

site_id	AH2
Number of Residues	5
Details	binding site for residues QUJ D 303 and QVE D 304

Chain	Residue
H	QUJ305
D	HIS4
D	LYS169
H	QVE306
D	ZN302

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	4
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	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":"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	8
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	4
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	4
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	8
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	4
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	8
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

site_id	MCSA3
Number of Residues	6
Details	M-CSA 216

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

site_id	MCSA4
Number of Residues	6
Details	M-CSA 216

Chain	Residue	Details
D	HIS64	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	HIS94	metal ligand
D	HIS96	metal ligand
D	GLU106	activator, electrostatic stabiliser, hydrogen bond acceptor
D	HIS119	metal ligand
D	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)