5THJ

Crystal Structure of 2-hydroxycyclohepta-2,4,6-trien-1-one bound to human carbonic anhydrase 2

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

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	0TR302

---

site_id	AC2
Number of Residues	10
Details	binding site for residue 0TR A 302

Chain	Residue
A	THR199
A	THR200
A	ZN301
A	HOH457
A	HOH580
A	HIS94
A	HIS96
A	HIS119
A	VAL121
A	LEU198

---

site_id	AC3
Number of Residues	7
Details	binding site for residue MBO A 303

Chain	Residue
A	VAL135
A	GLN136
A	GLN137
A	PRO138
A	GLU205
A	CYS206
A	HOH412

---

site_id	AC4
Number of Residues	5
Details	binding site for residue DMS A 304

Chain	Residue
A	SER99
A	LEU100
A	ASP101
A	ARG227
A	HOH471

---

site_id	AC5
Number of Residues	3
Details	binding site for residue DMS A 305

Chain	Residue
A	TYR7
A	ASP243
A	TRP245

---

site_id	AC6
Number of Residues	4
Details	binding site for residue DMS A 306

Chain	Residue
A	PRO83
A	THR208
A	HOH498
A	HOH606

---

site_id	AC7
Number of Residues	5
Details	binding site for residue DMS A 307

Chain	Residue
A	LYS159
A	PHE176
A	THR177
A	PHE179
A	HOH407

---

site_id	AC8
Number of Residues	5
Details	binding site for residue DMS A 308

Chain	Residue
A	TYR51
A	ASP52
A	ALA54
A	ASP180
A	HOH467

---

site_id	AC9
Number of Residues	5
Details	binding site for residue DMS A 309

Chain	Residue
A	TYR7
A	GLY8
A	VAL242
A	ASP243
A	HOH474

---

site_id	AD1
Number of Residues	2
Details	binding site for residue GOL A 310

Chain	Residue
A	ASN62
A	LYS170

---

site_id	AD2
Number of Residues	10
Details	binding site for residue CIT A 311

Chain	Residue
A	LYS111
A	LYS113
A	TYR128
A	LYS133
A	GLN137
A	HOH401
A	HOH482
A	HOH488
A	HOH521
A	HOH576

---

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	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962

Chain	Residue	Details
A	HIS64

---

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
A	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
A	HIS96
A	HIS119

---

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

Chain	Residue	Details
A	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
A	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
A	ASN62
A	ASN67

---

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
A	GLN92

---

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

Chain	Residue	Details
A	SER2

---

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

Chain	Residue	Details
A	SER166
A	SER173

---

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	THR199	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

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