6h6s

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	0016020	cellular_component	membrane
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	0016020	cellular_component	membrane
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	4
Details	binding site for residue NI A 301

Chain	Residue
A	HIS2
A	HIS3
A	TRP4
A	HOH455

site_id	AC2
Number of Residues	7
Details	binding site for residue NI A 302

Chain	Residue
A	HOH564
A	HOH589
A	HIS93
A	HIS95
A	HIS118
A	THR197
A	HOH401

site_id	AC3
Number of Residues	4
Details	binding site for residue NI B 301

Chain	Residue
B	HIS2
B	HIS3
B	TRP4
B	HOH408

site_id	AC4
Number of Residues	6
Details	binding site for residue NI B 302

Chain	Residue
B	HIS93
B	HIS95
B	HIS118
B	HOH402
B	HOH560
B	HOH596

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

Chain	Residue	Details
A	HIS63
B	HIS63

Chain	Residue	Details
B	HIS93
A	HIS93

Chain	Residue	Details
B	HIS95
B	HIS118
A	HIS95
A	HIS118

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10550681, ECO:0000269\|PubMed:19520834

Chain	Residue	Details
B	THR197
A	THR197

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	TYR6
B	TYR6

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
B	ASN61
B	ASN66
A	ASN61
A	ASN66

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	GLN91
B	GLN91

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P27139

Chain	Residue	Details
A	SER1
B	SER1

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER164
A	SER171
B	SER164
B	SER171

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	THR197	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	THR197	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)

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

Sad phasing on nickel-substituted human carbonic anhydrase II