5L9E

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

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	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	0006730	biological_process	one-carbon metabolic process
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
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	0016020	cellular_component	membrane
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	0016020	cellular_component	membrane
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	6H0302

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 307

Chain	Residue
A	HIS4
A	HIS64
A	QVE304
A	QVE306

---

site_id	AC3
Number of Residues	2
Details	binding site for residue ZN A 308

Chain	Residue
C	GLU26
A	HIS17

---

site_id	AC4
Number of Residues	3
Details	binding site for residue ZN A 309

Chain	Residue
A	ASP174
A	HOH443
C	HOH428

---

site_id	AC5
Number of Residues	3
Details	binding site for residue ZN A 310

Chain	Residue
A	ASP34
A	HIS36
A	HOH401

---

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN A 311

Chain	Residue
A	GLU186
A	HOH404
A	HOH433
B	ASP189

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN A 312

Chain	Residue
A	ASP52
A	HOH425
B	ASP52
B	HOH418

---

site_id	AC8
Number of Residues	1
Details	binding site for residue ZN A 313

Chain	Residue
A	HIS15

---

site_id	AC9
Number of Residues	6
Details	binding site for residue GOL A 314

Chain	Residue
A	ASN62
A	ALA65
A	ASN67
A	GLN92
A	6H0302
A	HOH406

---

site_id	AD1
Number of Residues	3
Details	binding site for residue ZN A 315

Chain	Residue
A	ASP189
A	LYS260
B	GLU186

---

site_id	AD2
Number of Residues	5
Details	binding site for residue ZN A 316

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

---

site_id	AD3
Number of Residues	4
Details	binding site for residue ZN B 301

Chain	Residue
B	HIS94
B	HIS96
B	HIS119
B	6H0302

---

site_id	AD4
Number of Residues	4
Details	binding site for residue ZN B 307

Chain	Residue
B	HIS4
B	HIS64
B	QVE304
B	QVE306

---

site_id	AD5
Number of Residues	3
Details	binding site for residue ZN B 308

Chain	Residue
B	HIS17
B	LYS18
D	GLU26

---

site_id	AD6
Number of Residues	2
Details	binding site for residue ZN B 309

Chain	Residue
B	ASP174
B	HOH427

---

site_id	AD7
Number of Residues	4
Details	binding site for residue ZN B 310

Chain	Residue
B	ASP34
B	HIS36
B	HOH401
B	HOH424

---

site_id	AD8
Number of Residues	5
Details	binding site for residue GOL B 311

Chain	Residue
B	ASN62
B	ALA65
B	ASN67
B	GLN92
B	6H0302

---

site_id	AD9
Number of Residues	4
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS94
C	HIS96
C	HIS119
C	6H0302

---

site_id	AE1
Number of Residues	5
Details	binding site for residue ZN C 307

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

---

site_id	AE2
Number of Residues	4
Details	binding site for residue ZN C 308

Chain	Residue
A	GLU26
A	HOH413
A	HOH417
C	HIS17

---

site_id	AE3
Number of Residues	2
Details	binding site for residue ZN C 309

Chain	Residue
C	ASP174
C	HOH427

---

site_id	AE4
Number of Residues	4
Details	binding site for residue ZN C 310

Chain	Residue
B	GLU14
C	ASP34
C	HIS36
C	HOH413

---

site_id	AE5
Number of Residues	4
Details	binding site for residue GOL C 311

Chain	Residue
C	ASN62
C	ASN67
C	HIS94
C	THR199

---

site_id	AE6
Number of Residues	3
Details	binding site for residue ZN C 312

Chain	Residue
B	HIS10
C	HIS36
C	HOH403

---

site_id	AE7
Number of Residues	4
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS94
D	HIS96
D	HIS119
D	6H0302

---

site_id	AE8
Number of Residues	4
Details	binding site for residue ZN D 306

Chain	Residue
D	HIS4
D	HIS64
D	QVE304
D	QVE305

---

site_id	AE9
Number of Residues	4
Details	binding site for residue ZN D 307

Chain	Residue
B	GLU26
B	HOH415
D	HIS17
D	HOH402

---

site_id	AF1
Number of Residues	2
Details	binding site for residue ZN D 308

Chain	Residue
B	HOH428
D	ASP174

---

site_id	AF2
Number of Residues	3
Details	binding site for residue ZN D 309

Chain	Residue
D	ASP34
D	HIS36
D	HOH425

---

site_id	AF3
Number of Residues	5
Details	binding site for residue GOL D 310

Chain	Residue
D	ASN62
D	ALA65
D	ASN67
D	GLN92
D	6H0302

---

site_id	AF4
Number of Residues	4
Details	binding site for residue ZN D 311

Chain	Residue
B	GLU233
B	GLU233
D	GLU233
D	GLU233

---

site_id	AF5
Number of Residues	14
Details	binding site for residues 6H0 A 302 and QUJ A 303

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
A	PHE130
A	LEU197
A	THR198
A	THR199
A	TRP208
A	ZN301
A	QVE304
A	QUJ305
A	QVE306
A	QVE306
A	GOL314

---

site_id	AF6
Number of Residues	7
Details	binding site for residues QUJ A 303 and QVE A 304

Chain	Residue
A	HIS4
A	LYS169
A	6H0302
A	6H0302
A	QUJ305
A	QVE306
A	ZN307

---

site_id	AF7
Number of Residues	10
Details	binding site for residues QVE A 304 and QUJ A 305

Chain	Residue
A	HIS4
A	ASP19
A	PHE20
A	LYS169
A	PRO201
A	6H0302
A	QUJ303
A	QVE306
A	ZN307
A	HOH419

---

site_id	AF8
Number of Residues	12
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
A	6H0302
A	6H0302
A	QUJ303
A	QVE304
A	ZN307
A	HOH419

---

site_id	AF9
Number of Residues	15
Details	binding site for residues 6H0 B 302 and QUJ B 303

Chain	Residue
B	HIS94
B	HIS96
B	HIS119
B	PHE130
B	LEU197
B	THR198
B	THR199
B	TRP208
B	ZN301
B	QVE304
B	QUJ305
B	QVE306
B	QVE306
B	GOL311
B	HOH421

---

site_id	AG1
Number of Residues	6
Details	binding site for residues QUJ B 303 and QVE B 304

Chain	Residue
B	HIS4
B	6H0302
B	6H0302
B	QUJ305
B	QVE306
B	ZN307

---

site_id	AG2
Number of Residues	8
Details	binding site for residues QVE B 304 and QUJ B 305

Chain	Residue
B	HIS4
B	ASP19
B	PHE20
B	6H0302
B	QUJ303
B	QVE306
B	ZN307
B	HOH414

---

site_id	AG3
Number of Residues	12
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
B	6H0302
B	6H0302
B	QUJ303
B	QVE304
B	ZN307
B	HOH414

---

site_id	AG4
Number of Residues	14
Details	binding site for residues QUJ B 312 and QVE D 304

Chain	Residue
B	HIS4
B	QUJ303
B	QUJ305
B	QVE306
B	ZN307
D	HIS4
D	ASP19
D	PHE20
D	LYS169
D	6H0302
D	QUJ303
D	QUJ303
D	QVE305
D	ZN306

---

site_id	AG5
Number of Residues	17
Details	binding site for residues QUJ B 312 and QVE D 305

Chain	Residue
B	ASP19
B	PHE20
B	6H0302
B	QUJ303
B	QVE304
B	QVE306
B	HOH414
D	HIS4
D	TRP5
D	ASP19
D	PHE20
D	HIS64
D	6H0302
D	6H0302
D	QUJ303
D	QVE304
D	ZN306

---

site_id	AG6
Number of Residues	13
Details	binding site for residues 6H0 C 302 and QUJ C 303

Chain	Residue
C	GLN92
C	HIS94
C	HIS96
C	HIS119
C	PHE130
C	LEU197
C	THR198
C	THR199
C	TRP208
C	ZN301
C	QVE304
C	QUJ305
C	QVE306

---

site_id	AG7
Number of Residues	8
Details	binding site for residues QUJ C 303 and QVE C 304

Chain	Residue
C	HIS4
C	LYS169
C	6H0302
C	6H0302
C	QUJ305
C	QVE306
C	ZN307
C	HOH401

---

site_id	AG8
Number of Residues	9
Details	binding site for residues QVE C 304 and QUJ C 305

Chain	Residue
C	HIS4
C	ASP19
C	PHE20
C	LYS169
C	6H0302
C	QUJ303
C	QVE306
C	ZN307
C	HOH401

---

site_id	AG9
Number of Residues	9
Details	binding site for residues QUJ C 305 and QVE C 306

Chain	Residue
C	HIS4
C	TRP5
C	ASP19
C	PHE20
C	HIS64
C	6H0302
C	QUJ303
C	QVE304
C	ZN307

---

site_id	AH1
Number of Residues	17
Details	binding site for residues 6H0 D 302 and QUJ D 303

Chain	Residue
B	QUJ312
D	GLN92
D	HIS94
D	HIS96
D	HIS119
D	PHE130
D	LEU197
D	THR198
D	THR199
D	TRP208
D	ZN301
D	QVE304
D	QVE304
D	QVE305
D	QVE305
D	GOL310
D	HOH406

---

site_id	AH2
Number of Residues	7
Details	binding site for residues QUJ D 303 and QVE D 304

Chain	Residue
B	QUJ312
D	HIS4
D	LYS169
D	6H0302
D	6H0302
D	QVE305
D	ZN306

---

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
A	HIS94
B	HIS94
C	HIS94
D	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
A	HIS96
A	HIS119
B	HIS96
B	HIS119
C	HIS96
C	HIS119
D	HIS96
D	HIS119

---

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

Chain	Residue	Details
A	THR198
B	THR198
C	THR198
D	THR198

---

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
A	TYR7
B	TYR7
C	TYR7
D	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
A	ASN62
A	ASN67
B	ASN62
B	ASN67
C	ASN62
C	ASN67
D	ASN62
D	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	SER165
A	SER172
B	SER165
B	SER172
C	SER165
C	SER172
D	SER165
D	SER172

---

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

---