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8DPO

Crystal structure of Neisseria gonorrhoeae carbonic anhydrase with Acetazolamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
C0004089molecular_functioncarbonate dehydratase activity
C0008270molecular_functionzinc ion binding
C0016829molecular_functionlyase activity
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
E0004089molecular_functioncarbonate dehydratase activity
E0008270molecular_functionzinc ion binding
E0016829molecular_functionlyase activity
E0042597cellular_componentperiplasmic space
E0046872molecular_functionmetal ion binding
G0004089molecular_functioncarbonate dehydratase activity
G0008270molecular_functionzinc ion binding
G0016829molecular_functionlyase activity
G0042597cellular_componentperiplasmic space
G0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SENqIkgrtFpmEAHFV
ChainResidueDetails
ASER97-VAL113

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues884
DetailsDomain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9761692","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-07-23

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