4lp6

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
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	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	21
Details	BINDING SITE FOR RESIDUE Q4I A 301

Chain	Residue
A	HIS94
A	TRP208
A	ZN310
A	HOH403
A	HOH424
A	HOH459
B	HIS4
B	TRP5
B	PHE20
B	HIS64
B	Q4I301
A	HIS96
B	ZN302
B	HOH453
A	HIS119
A	PHE130
A	VAL134
A	VAL142
A	LEU197
A	THR198
A	THR199

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 302

Chain	Residue
A	HIS4
A	HIS64
A	HOH426
B	Q4I301

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 303

Chain	Residue
A	LYS171
A	GLU233
A	HOH427
B	GLU26
B	ASP174

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 304

Chain	Residue
A	ASP174
A	HOH465
B	GLU233

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 305

Chain	Residue
A	HIS17
A	HOH466
A	HOH467
A	HOH468
A	HOH469

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 306

Chain	Residue
A	ASP34
A	HOH432
B	HIS36

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 307

Chain	Residue
A	HIS36
A	HOH431
B	ASP34

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 308

Chain	Residue
A	ASP72
A	HOH483
A	HOH484

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN A 309

Chain	Residue
A	GLU238
A	HOH477

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 310

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
A	Q4I301

site_id	BC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE Q4I B 301

Chain	Residue
A	HIS4
A	TRP5
A	ASP19
A	PHE20
A	HIS64
A	Q4I301
A	ZN302
A	HOH426
A	HOH452
B	HIS94
B	HIS96
B	HIS119
B	PHE130
B	VAL134
B	LEU197
B	THR198
B	THR199
B	TRP208
B	ZN305
B	HOH413
B	HOH418
B	HOH430
B	HOH438

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 302

Chain	Residue
A	Q4I301
B	HIS4
B	HIS64
B	HOH453

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN B 303

Chain	Residue
B	HIS17
B	HOH463

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 304

Chain	Residue
B	ASP72
B	HOH412
B	HOH454
B	HOH455

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 305

Chain	Residue
B	HIS94
B	HIS96
B	HIS119
B	Q4I301

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	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305\|PubMed:15667203, ECO:0000305\|PubMed:17330962

Chain	Residue	Details
A	HIS64
B	HIS64

Chain	Residue	Details
A	HIS94
B	HIS94

Chain	Residue	Details
A	HIS96
A	HIS119
B	HIS96
B	HIS119

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

Chain	Residue	Details
A	THR198
B	THR198

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	TYR7
B	TYR7

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
A	ASN62
A	ASN67
B	ASN62
B	ASN67

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	GLN92
B	GLN92

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

Chain	Residue	Details
A	SER2
B	SER2

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

Chain	Residue	Details
A	SER165
A	SER172
B	SER165
B	SER172

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	THR198	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	HIS64	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS94	metal ligand
B	HIS96	metal ligand
B	GLU106	activator, electrostatic stabiliser, hydrogen bond acceptor
B	HIS119	metal ligand
B	THR198	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)

Crystal Structure of Human Carbonic Anhydrase II in complex with a quinoline oligoamide foldamer