6Q3O
PROTEIN-AROMATIC FOLDAMER COMPLEX CRYSTAL STRUCTURE
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 |
C | 0002009 | biological_process | morphogenesis of an epithelium |
C | 0004064 | molecular_function | arylesterase activity |
C | 0004089 | molecular_function | carbonate dehydratase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0006730 | biological_process | one-carbon metabolic process |
C | 0008270 | molecular_function | zinc ion binding |
C | 0015670 | biological_process | carbon dioxide transport |
C | 0016829 | molecular_function | lyase activity |
C | 0018820 | molecular_function | cyanamide hydratase activity |
C | 0032230 | biological_process | positive regulation of synaptic transmission, GABAergic |
C | 0032849 | biological_process | positive regulation of cellular pH reduction |
C | 0038166 | biological_process | angiotensin-activated signaling pathway |
C | 0043209 | cellular_component | myelin sheath |
C | 0044070 | biological_process | regulation of monoatomic anion transport |
C | 0045177 | cellular_component | apical part of cell |
C | 0046872 | molecular_function | metal ion binding |
C | 0046903 | biological_process | secretion |
C | 0051453 | biological_process | regulation of intracellular pH |
C | 0070050 | biological_process | neuron cellular homeostasis |
C | 0070062 | cellular_component | extracellular exosome |
C | 2001150 | biological_process | positive regulation of dipeptide transmembrane transport |
C | 2001225 | biological_process | regulation of chloride transport |
D | 0002009 | biological_process | morphogenesis of an epithelium |
D | 0004064 | molecular_function | arylesterase activity |
D | 0004089 | molecular_function | carbonate dehydratase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0005886 | cellular_component | plasma membrane |
D | 0006730 | biological_process | one-carbon metabolic process |
D | 0008270 | molecular_function | zinc ion binding |
D | 0015670 | biological_process | carbon dioxide transport |
D | 0016829 | molecular_function | lyase activity |
D | 0018820 | molecular_function | cyanamide hydratase activity |
D | 0032230 | biological_process | positive regulation of synaptic transmission, GABAergic |
D | 0032849 | biological_process | positive regulation of cellular pH reduction |
D | 0038166 | biological_process | angiotensin-activated signaling pathway |
D | 0043209 | cellular_component | myelin sheath |
D | 0044070 | biological_process | regulation of monoatomic anion transport |
D | 0045177 | cellular_component | apical part of cell |
D | 0046872 | molecular_function | metal ion binding |
D | 0046903 | biological_process | secretion |
D | 0051453 | biological_process | regulation of intracellular pH |
D | 0070050 | biological_process | neuron cellular homeostasis |
D | 0070062 | cellular_component | extracellular exosome |
D | 2001150 | biological_process | positive regulation of dipeptide transmembrane transport |
D | 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 | QZS303 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue ZN A 306 |
Chain | Residue |
A | HIS4 |
A | HIS64 |
A | HOH567 |
A | HOH577 |
A | HOH580 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN A 307 |
Chain | Residue |
A | ASP189 |
A | HOH546 |
A | HOH574 |
B | GLU186 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN A 308 |
Chain | Residue |
A | HIS17 |
A | HOH555 |
A | HOH569 |
A | HOH572 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN A 309 |
Chain | Residue |
A | HIS15 |
A | ASP19 |
A | HOH566 |
A | HOH587 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue ZN A 310 |
Chain | Residue |
A | ASP129 |
A | LYS132 |
A | HOH523 |
C | ASP19 |
C | ZN310 |
C | HOH414 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN A 311 |
Chain | Residue |
A | GLU233 |
B | GLU233 |
C | GLU233 |
D | GLU233 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue ZN A 312 |
Chain | Residue |
A | ASP34 |
A | HIS36 |
A | HOH462 |
A | HOH544 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue ZN A 313 |
Chain | Residue |
A | ASP52 |
A | HOH537 |
B | ASP52 |
B | HOH517 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 314 |
Chain | Residue |
A | ASP72 |
A | HOH469 |
A | HOH553 |
A | HOH593 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue ZN B 301 |
Chain | Residue |
B | HIS94 |
B | HIS96 |
B | HIS119 |
B | QZS303 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue ZN B 306 |
Chain | Residue |
B | HIS4 |
B | TRP5 |
B | HIS64 |
B | HOH556 |
B | HOH568 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue ZN B 307 |
Chain | Residue |
A | GLU186 |
B | ASP189 |
B | HOH483 |
B | HOH557 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue ZN B 308 |
Chain | Residue |
B | HIS17 |
B | HOH555 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue ZN B 309 |
Chain | Residue |
B | ASP19 |
B | ZN310 |
D | ASP129 |
D | LYS132 |
D | HOH492 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue ZN B 310 |
Chain | Residue |
B | ASP19 |
B | ZN309 |
B | HOH511 |
B | HOH565 |
D | ASP129 |
D | HOH501 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue ZN B 311 |
Chain | Residue |
B | ASP34 |
B | HIS36 |
D | GLU14 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue ZN B 312 |
Chain | Residue |
B | ASP72 |
B | HOH475 |
B | HOH559 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue ZN C 301 |
Chain | Residue |
C | HIS94 |
C | HIS96 |
C | HIS119 |
C | QZS303 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue ZN C 306 |
Chain | Residue |
C | HIS4 |
C | TRP5 |
C | HIS64 |
C | HOH524 |
C | HOH531 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue ZN C 307 |
Chain | Residue |
C | HIS17 |
C | LYS18 |
C | HOH459 |
C | HOH530 |
site_id | AE4 |
Number of Residues | 5 |
Details | binding site for residue GOL C 308 |
Chain | Residue |
C | TYR7 |
C | PRO13 |
C | ASP242 |
C | TRP244 |
C | HOH401 |
site_id | AE5 |
Number of Residues | 3 |
Details | binding site for residue ZN C 309 |
Chain | Residue |
C | ASP34 |
C | HIS36 |
C | HOH510 |
site_id | AE6 |
Number of Residues | 3 |
Details | binding site for residue ZN C 310 |
Chain | Residue |
A | ZN310 |
C | ASP19 |
C | HOH414 |
site_id | AE7 |
Number of Residues | 4 |
Details | binding site for residue ZN D 301 |
Chain | Residue |
D | HIS94 |
D | HIS96 |
D | HIS119 |
D | QZS303 |
site_id | AE8 |
Number of Residues | 4 |
Details | binding site for residue ZN D 306 |
Chain | Residue |
D | HIS4 |
D | HIS64 |
D | HOH549 |
D | HOH554 |
site_id | AE9 |
Number of Residues | 3 |
Details | binding site for residue ZN D 307 |
Chain | Residue |
D | HIS17 |
D | HOH523 |
D | HOH545 |
site_id | AF1 |
Number of Residues | 2 |
Details | binding site for residue ZN D 308 |
Chain | Residue |
D | HIS15 |
D | ASP19 |
site_id | AF2 |
Number of Residues | 5 |
Details | binding site for residue ZN D 309 |
Chain | Residue |
D | ASP34 |
D | HIS36 |
D | HOH476 |
D | HOH503 |
D | HOH550 |
site_id | AF3 |
Number of Residues | 3 |
Details | binding site for residue ZN D 310 |
Chain | Residue |
D | ASP72 |
D | HOH555 |
D | HOH556 |
site_id | AF4 |
Number of Residues | 22 |
Details | binding site for residues QNL A 302 and QZS A 303 |
Chain | Residue |
A | PHE20 |
A | PRO21 |
A | ILE22 |
A | HIS94 |
A | HIS96 |
A | HIS119 |
A | PHE130 |
A | VAL134 |
A | GLN135 |
A | VAL142 |
A | LEU197 |
A | THR198 |
A | THR199 |
A | PRO201 |
A | LEU203 |
A | TRP208 |
A | ZN301 |
A | QUK304 |
A | QVE305 |
A | HOH434 |
A | HOH526 |
C | HIS4 |
site_id | AF5 |
Number of Residues | 26 |
Details | binding site for residues QZS A 303 and QUK A 304 |
Chain | Residue |
A | ASP19 |
A | PHE20 |
A | PRO21 |
A | HIS94 |
A | HIS96 |
A | HIS119 |
A | PHE130 |
A | VAL134 |
A | VAL142 |
A | LEU197 |
A | THR198 |
A | THR199 |
A | PRO201 |
A | LEU203 |
A | TRP208 |
A | ZN301 |
A | QNL302 |
A | QVE305 |
A | HOH434 |
A | HOH502 |
A | HOH526 |
B | HOH418 |
C | HIS4 |
C | QUK304 |
C | QVE305 |
D | QNL302 |
site_id | AF6 |
Number of Residues | 16 |
Details | binding site for residues QUK A 304 and QVE A 305 |
Chain | Residue |
A | ASP19 |
A | PRO21 |
A | LYS132 |
A | GLN135 |
A | QNL302 |
A | QZS303 |
A | HOH405 |
A | HOH451 |
A | HOH502 |
A | HOH517 |
B | HOH418 |
C | ASP19 |
C | QZS303 |
C | QUK304 |
C | QVE305 |
D | QNL302 |
site_id | AF7 |
Number of Residues | 25 |
Details | binding site for residues QNL B 302 and QZS B 303 |
Chain | Residue |
B | PRO21 |
B | ILE22 |
B | HIS94 |
B | HIS96 |
B | HIS119 |
B | PHE130 |
B | VAL134 |
B | GLN135 |
B | VAL142 |
B | LEU197 |
B | THR198 |
B | THR199 |
B | PRO201 |
B | LEU203 |
B | TRP208 |
B | ZN301 |
B | QUK304 |
B | QVE305 |
B | HOH411 |
B | HOH412 |
B | HOH455 |
B | HOH476 |
B | HOH495 |
B | HOH528 |
D | QVE305 |
site_id | AF8 |
Number of Residues | 26 |
Details | binding site for residues QZS B 303 and QUK B 304 |
Chain | Residue |
B | ASP19 |
B | PRO21 |
B | HIS94 |
B | HIS96 |
B | HIS119 |
B | PHE130 |
B | VAL134 |
B | VAL142 |
B | LEU197 |
B | THR198 |
B | THR199 |
B | PRO201 |
B | LEU203 |
B | TRP208 |
B | ZN301 |
B | QNL302 |
B | QVE305 |
B | HOH411 |
B | HOH412 |
B | HOH418 |
B | HOH455 |
B | HOH464 |
B | HOH476 |
B | HOH495 |
D | QUK304 |
D | QVE305 |
site_id | AF9 |
Number of Residues | 13 |
Details | binding site for residues QUK B 304 and QVE B 305 |
Chain | Residue |
B | ASP19 |
B | PRO21 |
B | GLY131 |
B | GLN135 |
B | QNL302 |
B | QZS303 |
B | HOH418 |
B | HOH464 |
B | HOH469 |
B | HOH515 |
D | QUK304 |
D | QVE305 |
D | HOH505 |
site_id | AG1 |
Number of Residues | 22 |
Details | binding site for residues QNL C 302 and QZS C 303 |
Chain | Residue |
A | QVE305 |
C | PHE20 |
C | PRO21 |
C | ILE22 |
C | GLN92 |
C | HIS94 |
C | HIS96 |
C | HIS119 |
C | VAL121 |
C | PHE130 |
C | VAL142 |
C | LEU197 |
C | THR198 |
C | THR199 |
C | PRO201 |
C | LEU203 |
C | TRP208 |
C | ZN301 |
C | QUK304 |
C | QVE305 |
C | HOH429 |
C | HOH507 |
site_id | AG2 |
Number of Residues | 25 |
Details | binding site for residues QZS C 303 and QUK C 304 |
Chain | Residue |
A | QUK304 |
A | QVE305 |
C | ASP19 |
C | PRO21 |
C | GLN92 |
C | HIS94 |
C | HIS96 |
C | HIS119 |
C | VAL121 |
C | PHE130 |
C | VAL142 |
C | LEU197 |
C | THR198 |
C | THR199 |
C | PRO201 |
C | LEU203 |
C | TRP208 |
C | ZN301 |
C | QNL302 |
C | QVE305 |
C | HOH429 |
C | HOH463 |
C | HOH487 |
C | HOH507 |
D | GLU26 |
site_id | AG3 |
Number of Residues | 11 |
Details | binding site for residues QUK C 304 and QVE C 305 |
Chain | Residue |
A | QUK304 |
A | QVE305 |
C | ASP19 |
C | PRO21 |
C | GLN135 |
C | QNL302 |
C | QZS303 |
C | HOH427 |
C | HOH463 |
C | HOH487 |
D | GLU26 |
site_id | AG4 |
Number of Residues | 25 |
Details | binding site for residues QNL D 302 and QZS D 303 |
Chain | Residue |
A | QUK304 |
B | HIS4 |
D | PHE20 |
D | PRO21 |
D | ILE22 |
D | GLN92 |
D | HIS94 |
D | HIS96 |
D | HIS119 |
D | PHE130 |
D | VAL134 |
D | GLN135 |
D | VAL142 |
D | LEU197 |
D | THR198 |
D | THR199 |
D | PRO201 |
D | LEU203 |
D | TRP208 |
D | ZN301 |
D | QUK304 |
D | QVE305 |
D | HOH419 |
D | HOH464 |
D | HOH495 |
site_id | AG5 |
Number of Residues | 28 |
Details | binding site for residues QZS D 303 and QUK D 304 |
Chain | Residue |
B | HIS4 |
B | QUK304 |
B | QVE305 |
D | ASP19 |
D | PRO21 |
D | GLN92 |
D | HIS94 |
D | HIS96 |
D | HIS119 |
D | PHE130 |
D | VAL134 |
D | VAL142 |
D | LEU197 |
D | THR198 |
D | THR199 |
D | PRO201 |
D | LEU203 |
D | TRP208 |
D | ZN301 |
D | QNL302 |
D | QVE305 |
D | HOH419 |
D | HOH464 |
D | HOH468 |
D | HOH489 |
D | HOH495 |
D | HOH524 |
D | HOH526 |
site_id | AG6 |
Number of Residues | 17 |
Details | binding site for residues QUK D 304 and QVE D 305 |
Chain | Residue |
B | ASP19 |
B | QZS303 |
B | QUK304 |
B | QVE305 |
D | ASP19 |
D | PRO21 |
D | LYS132 |
D | GLN135 |
D | QNL302 |
D | QZS303 |
D | HOH457 |
D | HOH468 |
D | HOH482 |
D | HOH489 |
D | HOH505 |
D | HOH524 |
D | HOH526 |
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 | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962 |
Chain | Residue | Details |
A | HIS64 | |
B | HIS64 | |
C | HIS64 | |
D | HIS64 |
Chain | Residue | Details |
A | HIS94 | |
B | HIS94 | |
C | HIS94 | |
D | HIS94 |
Chain | Residue | Details |
A | HIS96 | |
A | HIS119 | |
B | HIS96 | |
B | HIS119 | |
C | HIS96 | |
C | HIS119 | |
D | HIS96 | |
D | HIS119 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 |
Chain | Residue | Details |
A | THR198 | |
B | THR198 | |
C | THR198 | |
D | THR198 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962 |
Chain | Residue | Details |
A | TYR7 | |
B | TYR7 | |
C | TYR7 | |
D | TYR7 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
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 | |
C | ASN62 | |
C | ASN67 | |
D | ASN62 | |
D | ASN67 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
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 | |
C | GLN92 | |
D | GLN92 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139 |
Chain | Residue | Details |
A | SER2 | |
B | SER2 | |
C | SER2 | |
D | SER2 |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER165 | |
A | SER172 | |
B | SER165 | |
B | SER172 | |
C | SER165 | |
C | SER172 | |
D | SER165 | |
D | 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 |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 216 |
Chain | Residue | Details |
C | HIS64 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | HIS94 | metal ligand |
C | HIS96 | metal ligand |
C | GLU106 | activator, electrostatic stabiliser, hydrogen bond acceptor |
C | HIS119 | metal ligand |
C | THR198 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 216 |
Chain | Residue | Details |
D | HIS64 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | HIS94 | metal ligand |
D | HIS96 | metal ligand |
D | GLU106 | activator, electrostatic stabiliser, hydrogen bond acceptor |
D | HIS119 | metal ligand |
D | THR198 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity |