3F7B
Crystal Structure of soluble domain of CA4 in complex with small molecule.
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 | 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 | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 300 |
Chain | Residue |
A | HIS94 |
A | HIS96 |
A | HIS119 |
A | AG5302 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AG5 A 302 |
Chain | Residue |
A | GLN92 |
A | HIS94 |
A | HIS96 |
A | HIS119 |
A | VAL121 |
A | ILE141 |
A | LEU198 |
A | THR199 |
A | THR200 |
A | ZN300 |
A | HOH564 |
A | TYR7 |
A | ASN62 |
A | HIS64 |
A | SER65 |
A | MET67 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 301 |
Chain | Residue |
B | HIS94 |
B | HIS96 |
B | HIS119 |
B | AG5303 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE AG5 B 303 |
Chain | Residue |
A | SER128 |
A | HOH470 |
B | TYR7 |
B | ASN62 |
B | HIS64 |
B | SER65 |
B | GLN92 |
B | HIS94 |
B | HIS96 |
B | HIS119 |
B | VAL121 |
B | ILE141 |
B | LEU198 |
B | THR199 |
B | THR200 |
B | TRP209 |
B | ZN301 |
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 | 2 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"8942978","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Lipidation: {"description":"GPI-anchor amidated serine","evidences":[{"source":"PubMed","id":"7625839","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ca2 |
Chain | Residue | Details |
A | THR199 | |
A | HIS64 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ca2 |
Chain | Residue | Details |
B | THR199 | |
B | HIS64 |