1fsr

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	6
Details	BINDING SITE FOR RESIDUE CU A 262

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
A	THR199
A	HOH301
A	HOH302

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU B 263

Chain	Residue
B	THR199
B	HOH353
B	HOH354
B	HIS94
B	HIS96
B	HIS119

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

Chain	Residue	Details
A	HIS94
B	HIS94

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	THR199
B	THR199

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	SER166
A	SER173
B	SER166
B	SER173

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ca2

Chain	Residue	Details
A	THR199
A	HIS64

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ca2

Chain	Residue	Details
B	THR199
B	HIS64

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)

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

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

X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT