5JNA
Crystal structure for the complex of human carbonic anhydrase IV and topiramate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004089 | molecular_function | carbonate dehydratase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005791 | cellular_component | rough endoplasmic reticulum |
A | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005802 | cellular_component | trans-Golgi network |
A | 0005886 | cellular_component | plasma membrane |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009897 | cellular_component | external side of plasma membrane |
A | 0009986 | cellular_component | cell surface |
A | 0015701 | biological_process | bicarbonate transport |
A | 0016020 | cellular_component | membrane |
A | 0016323 | cellular_component | basolateral plasma membrane |
A | 0016324 | cellular_component | apical plasma membrane |
A | 0016829 | molecular_function | lyase activity |
A | 0030658 | cellular_component | transport vesicle membrane |
A | 0030667 | cellular_component | secretory granule membrane |
A | 0031526 | cellular_component | brush border membrane |
A | 0046872 | molecular_function | metal ion binding |
A | 0048471 | cellular_component | perinuclear region of cytoplasm |
A | 0070062 | cellular_component | extracellular exosome |
A | 0098552 | cellular_component | side of membrane |
B | 0004089 | molecular_function | carbonate dehydratase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005791 | cellular_component | rough endoplasmic reticulum |
B | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
B | 0005794 | cellular_component | Golgi apparatus |
B | 0005802 | cellular_component | trans-Golgi network |
B | 0005886 | cellular_component | plasma membrane |
B | 0006730 | biological_process | one-carbon metabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0009897 | cellular_component | external side of plasma membrane |
B | 0009986 | cellular_component | cell surface |
B | 0015701 | biological_process | bicarbonate transport |
B | 0016020 | cellular_component | membrane |
B | 0016323 | cellular_component | basolateral plasma membrane |
B | 0016324 | cellular_component | apical plasma membrane |
B | 0016829 | molecular_function | lyase activity |
B | 0030658 | cellular_component | transport vesicle membrane |
B | 0030667 | cellular_component | secretory granule membrane |
B | 0031526 | cellular_component | brush border membrane |
B | 0046872 | molecular_function | metal ion binding |
B | 0048471 | cellular_component | perinuclear region of cytoplasm |
B | 0070062 | cellular_component | extracellular exosome |
B | 0098552 | cellular_component | side of membrane |
C | 0004089 | molecular_function | carbonate dehydratase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005791 | cellular_component | rough endoplasmic reticulum |
C | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
C | 0005794 | cellular_component | Golgi apparatus |
C | 0005802 | cellular_component | trans-Golgi network |
C | 0005886 | cellular_component | plasma membrane |
C | 0006730 | biological_process | one-carbon metabolic process |
C | 0008270 | molecular_function | zinc ion binding |
C | 0009897 | cellular_component | external side of plasma membrane |
C | 0009986 | cellular_component | cell surface |
C | 0015701 | biological_process | bicarbonate transport |
C | 0016020 | cellular_component | membrane |
C | 0016323 | cellular_component | basolateral plasma membrane |
C | 0016324 | cellular_component | apical plasma membrane |
C | 0016829 | molecular_function | lyase activity |
C | 0030658 | cellular_component | transport vesicle membrane |
C | 0030667 | cellular_component | secretory granule membrane |
C | 0031526 | cellular_component | brush border membrane |
C | 0046872 | molecular_function | metal ion binding |
C | 0048471 | cellular_component | perinuclear region of cytoplasm |
C | 0070062 | cellular_component | extracellular exosome |
C | 0098552 | cellular_component | side of membrane |
D | 0004089 | molecular_function | carbonate dehydratase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005791 | cellular_component | rough endoplasmic reticulum |
D | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
D | 0005794 | cellular_component | Golgi apparatus |
D | 0005802 | cellular_component | trans-Golgi network |
D | 0005886 | cellular_component | plasma membrane |
D | 0006730 | biological_process | one-carbon metabolic process |
D | 0008270 | molecular_function | zinc ion binding |
D | 0009897 | cellular_component | external side of plasma membrane |
D | 0009986 | cellular_component | cell surface |
D | 0015701 | biological_process | bicarbonate transport |
D | 0016020 | cellular_component | membrane |
D | 0016323 | cellular_component | basolateral plasma membrane |
D | 0016324 | cellular_component | apical plasma membrane |
D | 0016829 | molecular_function | lyase activity |
D | 0030658 | cellular_component | transport vesicle membrane |
D | 0030667 | cellular_component | secretory granule membrane |
D | 0031526 | cellular_component | brush border membrane |
D | 0046872 | molecular_function | metal ion binding |
D | 0048471 | cellular_component | perinuclear region of cytoplasm |
D | 0070062 | cellular_component | extracellular exosome |
D | 0098552 | cellular_component | side of membrane |
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 | TOR302 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue TOR A 302 |
Chain | Residue |
A | HIS119 |
A | LEU198 |
A | THR199 |
A | THR200 |
A | ZN301 |
A | ASN62 |
A | SER65 |
A | GLN92 |
A | HIS94 |
A | HIS96 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 303 |
Chain | Residue |
A | ARG27 |
A | LEU195 |
A | ARG254 |
A | THR255 |
A | HOH451 |
A | HOH562 |
B | HOH547 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 304 |
Chain | Residue |
A | GLY50 |
A | TYR51 |
A | ASP52 |
A | LYS53 |
A | HOH516 |
A | HOH533 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue GOL A 305 |
Chain | Residue |
A | PHE48 |
A | SER50 |
A | SER78 |
A | ILE79 |
A | SER80 |
A | PRO87 |
C | GLN60 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue ZN B 301 |
Chain | Residue |
B | HIS94 |
B | HIS96 |
B | HIS119 |
B | TOR302 |
site_id | AC7 |
Number of Residues | 11 |
Details | binding site for residue TOR B 302 |
Chain | Residue |
B | ASN62 |
B | SER65 |
B | GLN92 |
B | HIS94 |
B | HIS96 |
B | HIS119 |
B | LEU198 |
B | THR199 |
B | THR200 |
B | ZN301 |
B | HOH514 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 303 |
Chain | Residue |
B | ARG27 |
B | LEU195 |
B | ARG254 |
B | THR255 |
B | HOH414 |
B | HOH483 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 304 |
Chain | Residue |
B | GLY50 |
B | TYR51 |
B | ASP52 |
B | LYS53 |
B | HOH455 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ACT B 305 |
Chain | Residue |
B | LYS15 |
D | GLN158 |
D | GLU162 |
D | HOH559 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue GOL B 306 |
Chain | Residue |
B | PHE48 |
B | SER50 |
B | SER78 |
B | ILE79 |
B | SER80 |
B | PRO87 |
D | GLN60 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue ZN C 301 |
Chain | Residue |
C | HIS94 |
C | HIS96 |
C | HIS119 |
C | TOR302 |
site_id | AD4 |
Number of Residues | 11 |
Details | binding site for residue TOR C 302 |
Chain | Residue |
C | ASN62 |
C | SER65 |
C | GLN92 |
C | HIS94 |
C | HIS96 |
C | HIS119 |
C | LEU198 |
C | THR199 |
C | THR200 |
C | ZN301 |
C | HOH550 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 303 |
Chain | Residue |
C | ARG27 |
C | ARG254 |
C | THR255 |
C | HOH463 |
C | HOH488 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue SO4 C 304 |
Chain | Residue |
C | GLY50 |
C | TYR51 |
C | ASP52 |
C | LYS53 |
C | HOH506 |
C | HOH511 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue ACT C 305 |
Chain | Residue |
C | ASN72 |
C | GLN89 |
A | ARG46 |
A | ARG189 |
site_id | AD8 |
Number of Residues | 9 |
Details | binding site for residue GOL C 306 |
Chain | Residue |
C | LYS103 |
C | ASP243 |
C | VAL245 |
C | PRO247 |
C | HOH441 |
C | HOH453 |
C | HOH485 |
C | HOH507 |
C | HOH548 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue ZN D 301 |
Chain | Residue |
D | HIS94 |
D | HIS96 |
D | HIS119 |
D | TOR302 |
site_id | AE1 |
Number of Residues | 10 |
Details | binding site for residue TOR D 302 |
Chain | Residue |
D | ASN62 |
D | SER65 |
D | GLN92 |
D | HIS94 |
D | HIS96 |
D | HIS119 |
D | LEU198 |
D | THR199 |
D | THR200 |
D | ZN301 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 303 |
Chain | Residue |
D | ARG27 |
D | ARG254 |
D | THR255 |
D | HOH505 |
D | HOH529 |
site_id | AE3 |
Number of Residues | 7 |
Details | binding site for residue SO4 D 304 |
Chain | Residue |
A | GLU2 |
D | GLY50 |
D | TYR51 |
D | ASP52 |
D | LYS53 |
D | HOH462 |
D | HOH477 |
site_id | AE4 |
Number of Residues | 10 |
Details | binding site for residue ACT D 305 |
Chain | Residue |
D | SER98 |
D | ASP99 |
D | LEU100 |
D | PRO101 |
D | ALA115 |
D | ALA150 |
D | ARG220 |
D | ILE223 |
D | LEU224 |
D | HOH449 |
Functional Information from PROSITE/UniProt
site_id | PS00162 |
Number of Residues | 17 |
Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHsLdgehFamEMHIV |
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:0000250|UniProtKB:P00918 |
Chain | Residue | Details |
A | HIS64 | |
B | HIS64 | |
C | HIS64 | |
D | HIS64 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8942978 |
Chain | Residue | Details |
A | HIS94 | |
D | HIS94 | |
D | HIS96 | |
D | HIS119 | |
A | HIS96 | |
A | HIS119 | |
B | HIS94 | |
B | HIS96 | |
B | HIS119 | |
C | HIS94 | |
C | HIS96 | |
C | HIS119 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00918 |
Chain | Residue | Details |
A | THR199 | |
B | THR199 | |
C | THR199 | |
D | THR199 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | LIPID: GPI-anchor amidated serine => ECO:0000269|PubMed:7625839 |
Chain | Residue | Details |
A | SER259 | |
B | SER259 | |
C | SER259 | |
D | SER259 |