5L70
CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH A QUINOLINE OLIGOAMIDE FOLDAMER
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 ZN A 301 |
Chain | Residue |
A | HIS94 |
A | HIS96 |
A | HIS119 |
A | 6H0302 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue ZN A 303 |
Chain | Residue |
A | HIS4 |
A | HIS64 |
A | QVS305 |
A | QVE307 |
A | HOH433 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue GOL A 304 |
Chain | Residue |
A | TRP5 |
A | ASN62 |
A | HIS64 |
A | THR199 |
A | PRO200 |
A | 6H0302 |
A | QVE307 |
A | HOH454 |
A | HOH520 |
A | HOH547 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue ZN A 308 |
Chain | Residue |
A | HIS17 |
A | HOH432 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue ZN A 309 |
Chain | Residue |
A | HIS36 |
A | ZN313 |
B | ASP34 |
B | HOH464 |
B | HOH502 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue ZN A 310 |
Chain | Residue |
A | ASP34 |
A | ZN313 |
A | HOH544 |
B | HIS36 |
B | HOH497 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue ZN A 311 |
Chain | Residue |
A | ASP174 |
A | HOH512 |
B | GLU233 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue ZN A 312 |
Chain | Residue |
A | GLU238 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue ZN A 313 |
Chain | Residue |
A | ZN309 |
A | ZN310 |
A | HOH544 |
B | HOH502 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 314 |
Chain | Residue |
A | ASP72 |
A | HOH552 |
A | HOH574 |
A | HOH594 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue GOL A 315 |
Chain | Residue |
A | THR35 |
A | ALA38 |
A | TRP191 |
A | PHE259 |
A | LYS260 |
A | HOH414 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue ZN B 302 |
Chain | Residue |
B | HIS94 |
B | HIS96 |
B | HIS119 |
B | 6H0303 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue ZN B 304 |
Chain | Residue |
A | QVS317 |
A | QVE319 |
A | HOH420 |
B | HIS4 |
B | HIS64 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue GOL B 305 |
Chain | Residue |
A | QVE319 |
B | TRP5 |
B | ASN62 |
B | THR199 |
B | PRO200 |
B | PRO201 |
B | 6H0303 |
B | HOH438 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue ZN B 306 |
Chain | Residue |
B | HIS17 |
B | HOH439 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue ZN B 307 |
Chain | Residue |
B | ASP72 |
B | HOH411 |
B | HOH512 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue GOL B 308 |
Chain | Residue |
B | THR35 |
B | ALA38 |
B | TRP191 |
B | PHE259 |
B | LYS260 |
site_id | AD9 |
Number of Residues | 21 |
Details | binding site for residues 6H0 A 302 and QOL A 316 |
Chain | Residue |
A | HIS94 |
A | HIS96 |
A | HIS119 |
A | VAL121 |
A | PHE130 |
A | VAL142 |
A | LEU197 |
A | THR198 |
A | THR199 |
A | TRP208 |
A | ZN301 |
A | GOL304 |
A | QVS305 |
A | QVE307 |
A | QVS317 |
A | QUK318 |
A | QVE319 |
A | HOH457 |
A | HOH543 |
B | QOL301 |
B | 6H0303 |
site_id | AE1 |
Number of Residues | 12 |
Details | binding site for residues QVS A 305 and QUK A 306 |
Chain | Residue |
A | PHE20 |
A | ZN303 |
A | QVE307 |
A | QOL316 |
A | QVS317 |
A | HOH433 |
A | HOH443 |
A | HOH480 |
B | QOL301 |
B | 6H0303 |
A | HIS4 |
A | ASP19 |
site_id | AE2 |
Number of Residues | 21 |
Details | binding site for residues QVS A 305 and QOL B 301 |
Chain | Residue |
A | HIS4 |
A | HIS94 |
A | HIS96 |
A | HIS119 |
A | 6H0302 |
A | ZN303 |
A | QUK306 |
A | QVE307 |
A | QOL316 |
A | QVS317 |
A | QVE319 |
A | HOH433 |
A | HOH480 |
B | TRP5 |
B | ASN62 |
B | THR199 |
B | PRO200 |
B | PRO201 |
B | 6H0303 |
B | HOH438 |
B | HOH449 |
site_id | AE3 |
Number of Residues | 15 |
Details | binding site for residues QUK A 306 and QVE A 307 |
Chain | Residue |
A | HIS4 |
A | TRP5 |
A | ASP19 |
A | PHE20 |
A | HIS64 |
A | 6H0302 |
A | ZN303 |
A | GOL304 |
A | QVS305 |
A | HOH423 |
A | HOH433 |
A | HOH443 |
A | HOH517 |
B | QOL301 |
B | 6H0303 |
site_id | AE4 |
Number of Residues | 10 |
Details | binding site for residues QOL A 316 and QVS A 317 |
Chain | Residue |
A | 6H0302 |
A | QVS305 |
A | QUK318 |
A | QVE319 |
A | HOH420 |
A | HOH543 |
B | HIS4 |
B | QOL301 |
B | 6H0303 |
B | ZN304 |
site_id | AE5 |
Number of Residues | 10 |
Details | binding site for residues QVS A 317 and QUK A 318 |
Chain | Residue |
A | 6H0302 |
A | QVS305 |
A | QOL316 |
A | QVE319 |
A | HOH420 |
B | HIS4 |
B | ASP19 |
B | PHE20 |
B | QOL301 |
B | ZN304 |
site_id | AE6 |
Number of Residues | 14 |
Details | binding site for residues QUK A 318 and QVE A 319 |
Chain | Residue |
A | 6H0302 |
A | QOL316 |
A | QVS317 |
A | HOH420 |
A | HOH504 |
A | HOH543 |
B | HIS4 |
B | TRP5 |
B | ASP19 |
B | PHE20 |
B | HIS64 |
B | 6H0303 |
B | ZN304 |
B | GOL305 |
site_id | AE7 |
Number of Residues | 22 |
Details | binding site for residues QOL B 301 and 6H0 B 303 |
Chain | Residue |
A | 6H0302 |
A | QVS305 |
A | QUK306 |
A | QVE307 |
A | QOL316 |
A | QVS317 |
A | QVE319 |
B | HIS94 |
B | HIS96 |
B | HIS119 |
B | VAL121 |
B | PHE130 |
B | VAL142 |
B | LEU197 |
B | THR198 |
B | THR199 |
B | PRO201 |
B | TRP208 |
B | ZN302 |
B | GOL305 |
B | HOH420 |
B | HOH449 |
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 |
B | HIS94 | |
A | HIS94 |
Chain | Residue | Details |
B | HIS96 | |
B | HIS119 | |
A | HIS96 | |
A | HIS119 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 |
Chain | Residue | Details |
B | THR198 | |
A | 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 |
B | ASN62 | |
B | ASN67 | |
A | ASN62 | |
A | 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 |