5L6T
CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH A QUINOLINE OLIGOAMIDE FOLDAMER
This is a non-PDB format compatible entry.
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 | 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 | 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 | 3 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS94 |
| A | HIS96 |
| A | HIS119 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | HIS4 |
| A | HIS64 |
| D | QVS304 |
| D | QVE306 |
| A | HOH402 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | HIS64 |
| A | THR199 |
| A | PRO200 |
| A | ASN62 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue ZN A 304 |
| Chain | Residue |
| A | HIS17 |
| A | HOH421 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 305 |
| Chain | Residue |
| A | HIS36 |
| A | ZN309 |
| B | ASP34 |
| B | HOH457 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 306 |
| Chain | Residue |
| A | ASP34 |
| A | ZN309 |
| A | HOH475 |
| B | HIS36 |
| B | HOH402 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 307 |
| Chain | Residue |
| A | ASP174 |
| A | HOH444 |
| A | HOH488 |
| B | HOH460 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue ZN A 308 |
| Chain | Residue |
| A | GLU238 |
| A | HOH463 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 309 |
| Chain | Residue |
| A | ZN305 |
| A | ZN306 |
| A | HOH475 |
| B | HOH457 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 310 |
| Chain | Residue |
| A | ASP72 |
| A | HOH409 |
| A | HOH412 |
| A | HOH428 |
| A | HOH470 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 311 |
| Chain | Residue |
| A | LYS171 |
| A | GLU233 |
| A | HOH401 |
| B | ASP174 |
| B | HOH431 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 312 |
| Chain | Residue |
| A | THR35 |
| A | ALA38 |
| A | TRP191 |
| A | PHE259 |
| A | LYS260 |
| A | HOH407 |
| A | HOH447 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| C | QVS304 |
| C | QVE306 |
| B | HIS4 |
| B | HIS64 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| C | QVE306 |
| B | ASN62 |
| B | THR199 |
| B | PRO200 |
| B | PRO201 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue ZN B 304 |
| Chain | Residue |
| B | HIS17 |
| B | HOH401 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue ZN B 305 |
| Chain | Residue |
| B | ASP72 |
| B | HOH404 |
| B | HOH424 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue ZN B 306 |
| Chain | Residue |
| B | ASP75 |
| B | ARG89 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 307 |
| Chain | Residue |
| B | THR35 |
| B | ALA38 |
| B | TRP191 |
| B | PHE259 |
| site_id | AE3 |
| Number of Residues | 10 |
| Details | binding site for residues QVS A 305 and QUK A 306 |
| Chain | Residue |
| A | HIS4 |
| A | ASP19 |
| A | PHE20 |
| A | ZN302 |
| D | QVE306 |
| C | QCL303 |
| C | QVS304 |
| D | HOH402 |
| D | HOH405 |
| D | QCL303 |
| site_id | AE4 |
| Number of Residues | 15 |
| Details | binding site for residues QVS A 305 and QCL B 301 |
| Chain | Residue |
| A | HIS4 |
| A | HIS94 |
| A | HIS96 |
| A | HIS119 |
| A | ZN302 |
| D | QUK305 |
| D | QVE306 |
| C | QCL303 |
| C | QVS304 |
| C | QVE306 |
| D | HOH402 |
| B | ASN62 |
| B | THR199 |
| B | PRO200 |
| B | PRO201 |
| site_id | AE5 |
| Number of Residues | 12 |
| Details | binding site for residues QUK A 306 and QVE A 307 |
| Chain | Residue |
| A | TRP5 |
| A | ASP19 |
| A | PHE20 |
| A | HIS64 |
| A | ZN302 |
| D | QVS304 |
| A | HOH402 |
| D | HOH401 |
| D | HOH403 |
| D | HOH405 |
| D | QCL303 |
| A | HIS4 |
| site_id | AE6 |
| Number of Residues | 6 |
| Details | binding site for residues QCL A 317 and QVS A 318 |
| Chain | Residue |
| D | QVS304 |
| C | QUK305 |
| C | QVE306 |
| B | HIS4 |
| D | QCL303 |
| B | ZN302 |
| site_id | AE7 |
| Number of Residues | 7 |
| Details | binding site for residues QVS A 318 and QUK A 319 |
| Chain | Residue |
| D | QVS304 |
| C | QCL303 |
| C | QVE306 |
| B | HIS4 |
| B | ASP19 |
| B | PHE20 |
| B | ZN302 |
| site_id | AE8 |
| Number of Residues | 9 |
| Details | binding site for residues QUK A 319 and QVE A 320 |
| Chain | Residue |
| C | QCL303 |
| C | QVS304 |
| B | HIS4 |
| B | TRP5 |
| B | ASP19 |
| B | PHE20 |
| B | HIS64 |
| B | ZN302 |
| B | GOL303 |
| site_id | AE9 |
| Number of Residues | 16 |
| Details | binding site for residues QCL B 301 and 6H0 B 303 |
| Chain | Residue |
| D | QVS304 |
| D | QUK305 |
| D | QVE306 |
| C | QCL303 |
| C | QVE306 |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| B | PHE130 |
| B | LEU197 |
| B | THR198 |
| B | THR199 |
| B | PRO201 |
| B | TRP208 |
| B | ZN301 |
| B | GOL303 |
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 |
