Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4QIY

Crystal structure of human carbonic anhydrase isozyme II with inhibitor

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	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	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	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	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	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	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	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	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	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
A	WWX302

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE WWX A 302

Chain	Residue
A	HIS119
A	PHE131
A	LEU198
A	THR199
A	THR200
A	PRO202
A	ZN301
A	ASN62
A	ASN67
A	GLN92
A	HIS94
A	HIS96

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS A 303

Chain	Residue
A	TYR7
A	ASP243
A	TRP245
A	PRO247
A	HOH616

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BCN A 304

Chain	Residue
A	LYS149
A	LYS213
A	GLU214
A	PRO215
A	HOH440
A	HOH639

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	HIS94
B	HIS96
B	HIS119
B	WWX302

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE WWX B 302

Chain	Residue
B	ASN62
B	ASN67
B	GLN92
B	HIS94
B	HIS96
B	HIS119
B	PHE131
B	LEU198
B	THR199
B	THR200
B	PRO202
B	ZN301

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMS B 303

Chain	Residue
B	TYR7
B	ASP243
B	TRP245
B	HOH631

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BCN B 304

Chain	Residue
B	LYS149
B	LYS213
B	GLU214
B	PRO215
B	HOH440
B	HOH461

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	HIS94
C	HIS96
C	HIS119
C	WWX302

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE WWX C 302

Chain	Residue
C	ASN62
C	ASN67
C	GLN92
C	HIS94
C	HIS96
C	HIS119
C	LEU198
C	THR199
C	THR200
C	PRO202
C	ZN301

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS C 303

Chain	Residue
C	ASP243
C	TRP245
C	HOH639

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BCN C 304

Chain	Residue
C	LYS149
C	LYS213
C	GLU214
C	PRO215
C	HOH440
C	HOH587
C	HOH640

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	HIS94
D	HIS96
D	HIS119
D	WWX302

site_id	BC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE WWX D 302

Chain	Residue
D	ASN62
D	ASN67
D	GLN92
D	HIS94
D	HIS96
D	HIS119
D	LEU141
D	LEU198
D	THR199
D	THR200
D	PRO202
D	ZN301

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMS D 303

Chain	Residue
D	TYR7
D	ASP243
D	TRP245
D	HOH637

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BCN D 304

Chain	Residue
D	LYS213
D	GLU214
D	PRO215
D	HOH440
D	HOH613
D	LYS149

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	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_FI2
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_FI3
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_FI4
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_FI5
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_FI6
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_FI7
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_FI8
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	768
Details	Domain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]}

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	THR199	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	THR199	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	THR199	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	THR199	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

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