3U3A

structure of Human Carbonic Anhydrase II V143I

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0002009	biological_process	morphogenesis of an epithelium
X	0004064	molecular_function	arylesterase activity
X	0004089	molecular_function	carbonate dehydratase activity
X	0005515	molecular_function	protein binding
X	0005737	cellular_component	cytoplasm
X	0005829	cellular_component	cytosol
X	0005886	cellular_component	plasma membrane
X	0006730	biological_process	one-carbon metabolic process
X	0008270	molecular_function	zinc ion binding
X	0015670	biological_process	carbon dioxide transport
X	0016020	cellular_component	membrane
X	0016829	molecular_function	lyase activity
X	0018820	molecular_function	cyanamide hydratase activity
X	0032230	biological_process	positive regulation of synaptic transmission, GABAergic
X	0032849	biological_process	positive regulation of cellular pH reduction
X	0038166	biological_process	angiotensin-activated signaling pathway
X	0043209	cellular_component	myelin sheath
X	0044070	biological_process	regulation of monoatomic anion transport
X	0045177	cellular_component	apical part of cell
X	0046872	molecular_function	metal ion binding
X	0046903	biological_process	secretion
X	0051453	biological_process	regulation of intracellular pH
X	0070050	biological_process	neuron cellular homeostasis
X	0070062	cellular_component	extracellular exosome
X	2001150	biological_process	positive regulation of dipeptide transmembrane transport
X	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 X 262

Chain	Residue
X	HIS94
X	HIS96
X	HIS119
X	HOH337

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL X 1304

Chain	Residue
X	TYR7
X	ASP243
X	TRP245
X	HOH434
X	HOH461

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL X 263

Chain	Residue
X	GLN92
X	PHE131
X	HOH300
X	HOH403
X	HOH449

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Functional Information from PROSITE/UniProt

site_id	PS00162
Number of Residues	17
Details	ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV

Chain	Residue	Details
X	SER105-VAL121

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962

Chain	Residue	Details
X	HIS64

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site_id	SWS_FT_FI2
Number of Residues	1
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
X	HIS94

---

site_id	SWS_FT_FI3
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: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
X	HIS96
X	HIS119

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834

Chain	Residue	Details
X	THR199

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962

Chain	Residue	Details
X	TYR7

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site_id	SWS_FT_FI6
Number of Residues	2
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
X	ASN62
X	ASN67

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site_id	SWS_FT_FI7
Number of Residues	1
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
X	GLN92

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139

Chain	Residue	Details
X	SER2

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site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
X	SER166
X	SER173

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 216

Chain	Residue	Details
X	HIS64	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
X	HIS94	metal ligand
X	HIS96	metal ligand
X	GLU106	activator, electrostatic stabiliser, hydrogen bond acceptor
X	HIS119	metal ligand
X	THR199	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

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