4YGJ
NaBr--Interactions between Hofmeister Anions and the Binding Pocket of a Protein
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS94 |
| A | HIS96 |
| A | HIS119 |
| A | BR302 |
| A | HOH647 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue BR A 302 |
| Chain | Residue |
| A | BR303 |
| A | HOH647 |
| A | HIS94 |
| A | HIS119 |
| A | THR199 |
| A | ZN301 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue BR A 303 |
| Chain | Residue |
| A | LEU198 |
| A | BR302 |
| A | BR304 |
| A | HOH647 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue BR A 304 |
| Chain | Residue |
| A | GLN92 |
| A | HIS94 |
| A | BR303 |
| A | HOH556 |
| A | HOH640 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue BR A 305 |
| Chain | Residue |
| A | HOH590 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue BR A 306 |
| Chain | Residue |
| A | PRO247 |
| A | GLN249 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue BR A 307 |
| Chain | Residue |
| A | LYS213 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue BR A 308 |
| Chain | Residue |
| A | PHE260 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue BR A 309 |
| Chain | Residue |
| A | HOH430 |
| A | HOH463 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue BR A 310 |
| Chain | Residue |
| A | LYS154 |
| A | ILE216 |
| A | SER217 |
| A | HOH508 |
| A | HOH661 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue BR A 311 |
| Chain | Residue |
| A | ASP165 |
| A | LYS228 |
| A | HOH577 |
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 | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962 |
| Chain | Residue | Details |
| A | HIS64 |
| Chain | Residue | Details |
| A | HIS94 |
| Chain | Residue | Details |
| A | HIS96 | |
| A | HIS119 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 |
| Chain | Residue | Details |
| A | THR199 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962 |
| Chain | Residue | Details |
| A | TYR7 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER166 | |
| A | SER173 |
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 | THR199 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity |
