4QIY

Crystal structure of human carbonic anhydrase isozyme II with inhibitor

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	0006730	biological_process	one-carbon metabolic process
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	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	0006730	biological_process	one-carbon metabolic process
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	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
C	0002009	biological_process	morphogenesis of an epithelium
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	0006730	biological_process	one-carbon metabolic process
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	0032230	biological_process	positive regulation of synaptic transmission, GABAergic
C	0032849	biological_process	positive regulation of cellular pH reduction
C	0038166	biological_process	angiotensin-activated signaling pathway
C	0043209	cellular_component	myelin sheath
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	0046903	biological_process	secretion
C	0051453	biological_process	regulation of intracellular pH
C	0070050	biological_process	neuron cellular homeostasis
C	0070062	cellular_component	extracellular exosome
C	2001150	biological_process	positive regulation of dipeptide transmembrane transport
C	2001225	biological_process	regulation of chloride transport
D	0002009	biological_process	morphogenesis of an epithelium
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	0006730	biological_process	one-carbon metabolic process
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	0032230	biological_process	positive regulation of synaptic transmission, GABAergic
D	0032849	biological_process	positive regulation of cellular pH reduction
D	0038166	biological_process	angiotensin-activated signaling pathway
D	0043209	cellular_component	myelin sheath
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	0046903	biological_process	secretion
D	0051453	biological_process	regulation of intracellular pH
D	0070050	biological_process	neuron cellular homeostasis
D	0070062	cellular_component	extracellular exosome
D	2001150	biological_process	positive regulation of dipeptide transmembrane transport
D	2001225	biological_process	regulation of chloride 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	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962

Chain	Residue	Details
A	HIS64
B	HIS64
C	HIS64
D	HIS64

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:4621826, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942

Chain	Residue	Details
B	HIS94
C	HIS94
D	HIS94
A	HIS94

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942

Chain	Residue	Details
C	HIS96
C	HIS119
D	HIS96
D	HIS119
B	HIS96
B	HIS119
A	HIS96
A	HIS119

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834

Chain	Residue	Details
B	THR199
C	THR199
D	THR199
A	THR199

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962

Chain	Residue	Details
C	TYR7
D	TYR7
A	TYR7
B	TYR7

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	SITE: Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962

Chain	Residue	Details
C	ASN62
C	ASN67
D	ASN62
D	ASN67
A	ASN62
A	ASN67
B	ASN62
B	ASN67

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	SITE: Involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962

Chain	Residue	Details
A	GLN92
B	GLN92
C	GLN92
D	GLN92

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139

Chain	Residue	Details
A	SER2
B	SER2
C	SER2
D	SER2

---

site_id	SWS_FT_FI9
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER166
A	SER173
B	SER166
B	SER173
C	SER166
C	SER173
D	SER166
D	SER173

---

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

---