4LP6
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 | 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 |