5L3O

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	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

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	6
Details	binding site for residue GOL A 302

Chain	Residue
A	ASN62
A	ASN67
A	GLN92
A	HIS94
A	HIS96
A	HOH402

---

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL A 303

Chain	Residue
A	HIS4
A	ASN11
A	HIS15
A	TRP16
A	LYS18
A	ASP19

---

site_id	AC4
Number of Residues	4
Details	binding site for residue GOL A 304

Chain	Residue
A	TYR7
A	ASP242
A	TRP244
A	PRO246

---

site_id	AC5
Number of Residues	8
Details	binding site for residue QUK E 306

Chain	Residue
C	QUK304
F	QUJ310
F	QVS312
E	QVE308
F	QUK311
F	QVE313
E	QUJ305
E	QVS307

---

site_id	AC6
Number of Residues	10
Details	binding site for residue QVS E 307

Chain	Residue
F	QUJ310
F	QVS312
E	QUK306
E	QVE308
F	QUK311
F	QVE313
D	QUJ309
E	QUJ305
D	QUK310
E	HOH401

---

site_id	AC7
Number of Residues	3
Details	binding site for residue ZN B 301

Chain	Residue
B	HIS94
B	HIS96
B	HIS119

---

site_id	AC8
Number of Residues	10
Details	binding site for residue GOL B 302

Chain	Residue
B	TYR7
B	ASN62
B	HIS64
B	ALA65
B	ASN67
B	GLN92
B	HIS94
B	HIS96
B	THR199
B	HOH410

---

site_id	AC9
Number of Residues	6
Details	binding site for residue GOL B 303

Chain	Residue
B	HIS4
B	ASN11
B	HIS15
B	TRP16
B	LYS18
B	ASP19

---

site_id	AD1
Number of Residues	6
Details	binding site for residue GOL B 304

Chain	Residue
B	TYR7
B	ASP242
B	TRP244
B	PRO246
B	HOH407
B	HOH463

---

site_id	AD2
Number of Residues	6
Details	binding site for residue GOL B 305

Chain	Residue
B	LEU163
B	ASP164
B	LYS167
B	LYS224
B	LYS227
B	LEU228

---

site_id	AD4
Number of Residues	12
Details	binding site for residues QUK A 303 and QVS A 304

Chain	Residue
A	HIS3
A	PHE20
C	QVE306
F	QVS312
C	QUJ303
E	QUK306
C	HOH404
B	ASP129
B	LYS132
F	QVE313
E	QUJ305
B	HOH428

---

site_id	AD5
Number of Residues	9
Details	binding site for residues QUK A 303 and QUJ A 312

Chain	Residue
A	HIS3
C	QVS305
C	QVE306
F	QVS312
E	QUK306
C	HOH404
B	GLY131
F	QVE313
E	QUJ305

---

site_id	AD6
Number of Residues	10
Details	binding site for residues QVS A 304 and QVE A 305

Chain	Residue
A	SER2
A	HIS3
A	PHE20
C	QUK304
C	QUJ303
C	HOH402
C	HOH403
B	ASP129
B	LYS132
B	HOH428

---

site_id	AE1
Number of Residues	17
Details	binding site for residues QUJ A 310 and QUK B 301

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
A	ASP129
A	LYS132
F	QVS312
E	QUK306
E	QVE308
B	HIS3
B	ASP19
B	PHE20
F	QVE313
D	QUJ309
E	QUJ305
E	QVS307
D	QUK310
D	QVE312

---

site_id	AE2
Number of Residues	29
Details	binding site for residues QVS A 311 and QVE B 302

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
A	PHE130
A	VAL142
A	LEU197
A	THR198
A	THR199
A	PRO201
A	TRP208
A	ZN301
C	QUK304
C	QVS305
F	QUJ310
C	QUJ303
E	QUK306
E	QVE308
C	HOH401
C	HOH405
C	HOH406
B	SER2
B	HIS3
F	QUK311
D	QUJ309
E	QUJ305
E	QVS307
D	QUK310
D	QVS311
D	HOH402

---

site_id	AE3
Number of Residues	17
Details	binding site for residues QVS A 311 and QUK B 301

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
C	QUK304
F	QUJ310
C	QUJ303
E	QUK306
E	QVE308
B	SER2
B	HIS3
F	QVE313
D	QUJ309
E	QUJ305
E	QVS307
D	QUK310
D	QVS311
D	HOH402

---

site_id	AE4
Number of Residues	9
Details	binding site for residues QVE B 302 and 6H0 B 304

Chain	Residue
C	QUK304
F	QUJ310
F	QVS312
C	QUJ303
E	QUK306
E	QVE308
F	QUK311
E	QUJ305
E	QVS307

---

site_id	AE5
Number of Residues	9
Details	binding site for residues QVE B 302 and 6H0 B 304

Chain	Residue
C	QUK304
F	QUJ310
F	QVS312
C	QUJ303
E	QUK306
E	QVE308
F	QUK311
E	QUJ305
E	QVS307

---

site_id	AE6
Number of Residues	9
Details	binding site for residues QVE B 302 and 6H0 B 304

Chain	Residue
C	QUK304
F	QUJ310
F	QVS312
C	QUJ303
E	QUK306
E	QVE308
F	QUK311
E	QUJ305
E	QVS307

---

site_id	AE7
Number of Residues	21
Details	binding site for residues QUJ B 303 and 6H0 B 308

Chain	Residue
A	GLY131
F	QUJ310
E	QVE308
B	HIS94
B	HIS96
B	HIS119
B	PHE130
B	LEU197
B	THR198
B	THR199
B	PRO201
B	TRP208
F	QVE313
E	QUJ305
E	QVS307
B	ZN301
D	QUK310
D	QVS311
D	QVE312
B	HOH406
D	HOH401

---

site_id	AE8
Number of Residues	10
Details	binding site for residues QUJ B 303 and QUK B 309

Chain	Residue
A	GLY131
F	QUJ310
E	QVE308
B	HIS3
F	QUK311
E	QVS307
D	QVS311
D	QVE312
B	HOH454
D	HOH403

---

site_id	AF1
Number of Residues	13
Details	binding site for residues QUK B 309 and QVS B 310

Chain	Residue
A	ASP129
A	LYS132
F	QUJ310
E	QVE308
B	HIS3
B	ASP19
B	PHE20
F	QUK311
D	QUJ309
E	QVS307
D	QVE312
B	HOH454
D	HOH403

---

site_id	AF2
Number of Residues	9
Details	binding site for residues QVS B 310 and QVE B 311

Chain	Residue
A	ASP129
A	LYS132
B	SER2
B	HIS3
B	ASP19
B	PHE20
D	QUJ309
D	QUK310
D	HOH402

---

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	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962

Chain	Residue	Details
A	HIS64
B	HIS64

---

site_id	SWS_FT_FI2
Number of Residues	2
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

---

site_id	SWS_FT_FI3
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: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

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834

Chain	Residue	Details
A	THR198
B	THR198

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962

Chain	Residue	Details
A	TYR7
B	TYR7

---

site_id	SWS_FT_FI6
Number of Residues	4
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

---

site_id	SWS_FT_FI7
Number of Residues	2
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

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139

Chain	Residue	Details
A	SER2
B	SER2

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER165
A	SER172
B	SER165
B	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

---