Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NJ6

Thermostable variant of human carbonic anhydrase with tetrazine 2.0 at site 186 reacted with sTCO in crystallo

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	0038166	biological_process	angiotensin-activated signaling pathway
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	0051453	biological_process	regulation of intracellular pH
A	0070062	cellular_component	extracellular exosome
A	2001150	biological_process	positive regulation of dipeptide transmembrane transport
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	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	0038166	biological_process	angiotensin-activated signaling pathway
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	0051453	biological_process	regulation of intracellular pH
B	0070062	cellular_component	extracellular exosome
B	2001150	biological_process	positive regulation of dipeptide transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue SO4 A 302

Chain	Residue
A	ALA37
A	LYS38
A	TYR39
A	HIS261
A	HOH426
A	HOH546

site_id	AC2
Number of Residues	6
Details	binding site for residue GOL A 303

Chain	Residue
A	HOH502
A	HOH589
A	HOH615
A	ASN66
A	GLU68
A	GLN91

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL A 304

Chain	Residue
A	PRO45
A	LEU46
A	LEU188
A	ASP189
A	SER258
A	HOH410
A	HOH430

site_id	AC4
Number of Residues	6
Details	binding site for residue GOL A 305

Chain	Residue
A	TRP4
A	PHE19
A	PRO201
A	HOH413
A	HOH557
A	HOH733

site_id	AC5
Number of Residues	5
Details	binding site for residue ZN A 306

Chain	Residue
A	HIS93
A	HIS95
A	HIS118
A	SO4307
A	HOH407

site_id	AC6
Number of Residues	10
Details	binding site for residue SO4 A 307

Chain	Residue
A	HIS93
A	HIS95
A	HIS118
A	LEU197
A	THR198
A	ZN306
A	HOH401
A	HOH407
A	HOH414
A	HOH595

site_id	AC7
Number of Residues	7
Details	binding site for residue SO4 B 302

Chain	Residue
A	LYS171
A	HOH423
B	GLY170
B	LYS171
B	SER172
B	HOH431
B	HOH492

site_id	AC8
Number of Residues	4
Details	binding site for residue SO4 B 303

Chain	Residue
B	LYS38
B	TYR39
B	HIS261
B	HOH401

site_id	AC9
Number of Residues	7
Details	binding site for residue GOL B 304

Chain	Residue
B	ASN66
B	GLU68
B	GLN91
B	PHE130
B	GOL305
B	HOH408
B	HOH420

site_id	AD1
Number of Residues	8
Details	binding site for residue GOL B 305

Chain	Residue
B	ASN61
B	ASN66
B	GLN91
B	GOL304
B	HOH420
B	HOH489
B	HOH515
B	HOH604

site_id	AD2
Number of Residues	5
Details	binding site for residue ZN B 306

Chain	Residue
B	HIS93
B	HIS95
B	HIS118
B	SO4307
B	HOH446

site_id	AD3
Number of Residues	12
Details	binding site for residue SO4 B 307

Chain	Residue
B	HIS93
B	HIS95
B	HIS118
B	LEU197
B	THR198
B	THR199
B	ZN306
B	HOH402
B	HOH446
B	HOH489
B	HOH543
B	HOH607

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	SER104-VAL120

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15667203","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11076507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12499545","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1336460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1433293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1909891","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19583303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151020","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4621826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7803386","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7901850","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8218160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8262987","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8399159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8431430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8451242","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8482389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8639494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8987974","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9865942","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11076507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12499545","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1336460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1433293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1909891","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19583303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151020","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7803386","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7901850","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8218160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8262987","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8399159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8431430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8451242","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8482389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8639494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8987974","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9865942","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10550681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19520834","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Site: {"description":"Fine-tunes the proton-transfer properties of H-64","evidences":[{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Site: {"description":"Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine","evidences":[{"source":"PubMed","id":"16214338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9265618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Site: {"description":"Involved in the binding of some activators, including histamine and L-histidine","evidences":[{"source":"PubMed","id":"16214338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9265618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 216

Chain	Residue	Details
A	HIS63	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS93	metal ligand
A	HIS95	metal ligand
A	GLU105	activator, electrostatic stabiliser, hydrogen bond acceptor
A	HIS118	metal ligand
A	LEU202	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	HIS63	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS93	metal ligand
B	HIS95	metal ligand
B	GLU105	activator, electrostatic stabiliser, hydrogen bond acceptor
B	HIS118	metal ligand
B	LEU202	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)
		EDMap 2fo-fc (MTZ)