8BZZ

Crystal structure of carbonic anhydrase 2 4-(dimethylamino)-N-nitrobenzenesulfonamide

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
AAA	0002009	biological_process	morphogenesis of an epithelium
AAA	0004064	molecular_function	arylesterase activity
AAA	0004089	molecular_function	carbonate dehydratase activity
AAA	0005515	molecular_function	protein binding
AAA	0005737	cellular_component	cytoplasm
AAA	0005829	cellular_component	cytosol
AAA	0005886	cellular_component	plasma membrane
AAA	0006730	biological_process	one-carbon metabolic process
AAA	0008270	molecular_function	zinc ion binding
AAA	0015670	biological_process	carbon dioxide transport
AAA	0016829	molecular_function	lyase activity
AAA	0018820	molecular_function	cyanamide hydratase activity
AAA	0032230	biological_process	positive regulation of synaptic transmission, GABAergic
AAA	0032849	biological_process	positive regulation of cellular pH reduction
AAA	0038166	biological_process	angiotensin-activated signaling pathway
AAA	0043209	cellular_component	myelin sheath
AAA	0044070	biological_process	regulation of monoatomic anion transport
AAA	0045177	cellular_component	apical part of cell
AAA	0046872	molecular_function	metal ion binding
AAA	0046903	biological_process	secretion
AAA	0051453	biological_process	regulation of intracellular pH
AAA	0070050	biological_process	neuron cellular homeostasis
AAA	0070062	cellular_component	extracellular exosome
AAA	2001150	biological_process	positive regulation of dipeptide transmembrane transport
AAA	2001225	biological_process	regulation of chloride transport

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
AAA	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
AAA	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
AAA	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
AAA	HIS96
AAA	HIS119

---

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

Chain	Residue	Details
AAA	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
AAA	TYR7

---

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
AAA	ASN62
AAA	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
AAA	GLN92

---

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

Chain	Residue	Details
AAA	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
AAA	SER166
AAA	SER173

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 216

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

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