5L3O
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 | 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 | 3 |
Details | binding site for residue ZN A 301 |
Chain | Residue |
A | HIS94 |
A | HIS96 |
A | HIS119 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
A | ASN62 |
A | ASN67 |
A | GLN92 |
A | HIS94 |
A | HIS96 |
A | HOH402 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue GOL A 303 |
Chain | Residue |
A | HIS4 |
A | ASN11 |
A | HIS15 |
A | TRP16 |
A | LYS18 |
A | ASP19 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue GOL A 304 |
Chain | Residue |
A | TYR7 |
A | ASP242 |
A | TRP244 |
A | PRO246 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue QUK E 306 |
Chain | Residue |
C | QUK304 |
F | QUJ310 |
F | QVS312 |
E | QVE308 |
F | QUK311 |
F | QVE313 |
E | QUJ305 |
E | QVS307 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue QVS E 307 |
Chain | Residue |
F | QUJ310 |
F | QVS312 |
E | QUK306 |
E | QVE308 |
F | QUK311 |
F | QVE313 |
D | QUJ309 |
E | QUJ305 |
D | QUK310 |
E | HOH401 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue ZN B 301 |
Chain | Residue |
B | HIS94 |
B | HIS96 |
B | HIS119 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue GOL B 302 |
Chain | Residue |
B | TYR7 |
B | ASN62 |
B | HIS64 |
B | ALA65 |
B | ASN67 |
B | GLN92 |
B | HIS94 |
B | HIS96 |
B | THR199 |
B | HOH410 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue GOL B 303 |
Chain | Residue |
B | HIS4 |
B | ASN11 |
B | HIS15 |
B | TRP16 |
B | LYS18 |
B | ASP19 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue GOL B 304 |
Chain | Residue |
B | TYR7 |
B | ASP242 |
B | TRP244 |
B | PRO246 |
B | HOH407 |
B | HOH463 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue GOL B 305 |
Chain | Residue |
B | LEU163 |
B | ASP164 |
B | LYS167 |
B | LYS224 |
B | LYS227 |
B | LEU228 |
site_id | AD4 |
Number of Residues | 12 |
Details | binding site for residues QUK A 303 and QVS A 304 |
Chain | Residue |
A | HIS3 |
A | PHE20 |
C | QVE306 |
F | QVS312 |
C | QUJ303 |
E | QUK306 |
C | HOH404 |
B | ASP129 |
B | LYS132 |
F | QVE313 |
E | QUJ305 |
B | HOH428 |
site_id | AD5 |
Number of Residues | 9 |
Details | binding site for residues QUK A 303 and QUJ A 312 |
Chain | Residue |
A | HIS3 |
C | QVS305 |
C | QVE306 |
F | QVS312 |
E | QUK306 |
C | HOH404 |
B | GLY131 |
F | QVE313 |
E | QUJ305 |
site_id | AD6 |
Number of Residues | 10 |
Details | binding site for residues QVS A 304 and QVE A 305 |
Chain | Residue |
A | SER2 |
A | HIS3 |
A | PHE20 |
C | QUK304 |
C | QUJ303 |
C | HOH402 |
C | HOH403 |
B | ASP129 |
B | LYS132 |
B | HOH428 |
site_id | AE1 |
Number of Residues | 17 |
Details | binding site for residues QUJ A 310 and QUK B 301 |
Chain | Residue |
A | HIS94 |
A | HIS96 |
A | HIS119 |
A | ASP129 |
A | LYS132 |
F | QVS312 |
E | QUK306 |
E | QVE308 |
B | HIS3 |
B | ASP19 |
B | PHE20 |
F | QVE313 |
D | QUJ309 |
E | QUJ305 |
E | QVS307 |
D | QUK310 |
D | QVE312 |
site_id | AE2 |
Number of Residues | 29 |
Details | binding site for residues QVS A 311 and QVE B 302 |
Chain | Residue |
A | HIS94 |
A | HIS96 |
A | HIS119 |
A | PHE130 |
A | VAL142 |
A | LEU197 |
A | THR198 |
A | THR199 |
A | PRO201 |
A | TRP208 |
A | ZN301 |
C | QUK304 |
C | QVS305 |
F | QUJ310 |
C | QUJ303 |
E | QUK306 |
E | QVE308 |
C | HOH401 |
C | HOH405 |
C | HOH406 |
B | SER2 |
B | HIS3 |
F | QUK311 |
D | QUJ309 |
E | QUJ305 |
E | QVS307 |
D | QUK310 |
D | QVS311 |
D | HOH402 |
site_id | AE3 |
Number of Residues | 17 |
Details | binding site for residues QVS A 311 and QUK B 301 |
Chain | Residue |
A | HIS94 |
A | HIS96 |
A | HIS119 |
C | QUK304 |
F | QUJ310 |
C | QUJ303 |
E | QUK306 |
E | QVE308 |
B | SER2 |
B | HIS3 |
F | QVE313 |
D | QUJ309 |
E | QUJ305 |
E | QVS307 |
D | QUK310 |
D | QVS311 |
D | HOH402 |
site_id | AE4 |
Number of Residues | 9 |
Details | binding site for residues QVE B 302 and 6H0 B 304 |
Chain | Residue |
C | QUK304 |
F | QUJ310 |
F | QVS312 |
C | QUJ303 |
E | QUK306 |
E | QVE308 |
F | QUK311 |
E | QUJ305 |
E | QVS307 |
site_id | AE5 |
Number of Residues | 9 |
Details | binding site for residues QVE B 302 and 6H0 B 304 |
Chain | Residue |
C | QUK304 |
F | QUJ310 |
F | QVS312 |
C | QUJ303 |
E | QUK306 |
E | QVE308 |
F | QUK311 |
E | QUJ305 |
E | QVS307 |
site_id | AE6 |
Number of Residues | 9 |
Details | binding site for residues QVE B 302 and 6H0 B 304 |
Chain | Residue |
C | QUK304 |
F | QUJ310 |
F | QVS312 |
C | QUJ303 |
E | QUK306 |
E | QVE308 |
F | QUK311 |
E | QUJ305 |
E | QVS307 |
site_id | AE7 |
Number of Residues | 21 |
Details | binding site for residues QUJ B 303 and 6H0 B 308 |
Chain | Residue |
A | GLY131 |
F | QUJ310 |
E | QVE308 |
B | HIS94 |
B | HIS96 |
B | HIS119 |
B | PHE130 |
B | LEU197 |
B | THR198 |
B | THR199 |
B | PRO201 |
B | TRP208 |
F | QVE313 |
E | QUJ305 |
E | QVS307 |
B | ZN301 |
D | QUK310 |
D | QVS311 |
D | QVE312 |
B | HOH406 |
D | HOH401 |
site_id | AE8 |
Number of Residues | 10 |
Details | binding site for residues QUJ B 303 and QUK B 309 |
Chain | Residue |
A | GLY131 |
F | QUJ310 |
E | QVE308 |
B | HIS3 |
F | QUK311 |
E | QVS307 |
D | QVS311 |
D | QVE312 |
B | HOH454 |
D | HOH403 |
site_id | AF1 |
Number of Residues | 13 |
Details | binding site for residues QUK B 309 and QVS B 310 |
Chain | Residue |
A | ASP129 |
A | LYS132 |
F | QUJ310 |
E | QVE308 |
B | HIS3 |
B | ASP19 |
B | PHE20 |
F | QUK311 |
D | QUJ309 |
E | QVS307 |
D | QVE312 |
B | HOH454 |
D | HOH403 |
site_id | AF2 |
Number of Residues | 9 |
Details | binding site for residues QVS B 310 and QVE B 311 |
Chain | Residue |
A | ASP129 |
A | LYS132 |
B | SER2 |
B | HIS3 |
B | ASP19 |
B | PHE20 |
D | QUJ309 |
D | QUK310 |
D | HOH402 |
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 |