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8DR2

Crystal structure of Neisseria gonorrhoeae carbonic anhydrase with 2-cyclohexyl-N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)acetamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0006885biological_processregulation of pH
A0008270molecular_functionzinc ion binding
A0015670biological_processcarbon dioxide transport
A0016829molecular_functionlyase activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
C0004089molecular_functioncarbonate dehydratase activity
C0006885biological_processregulation of pH
C0008270molecular_functionzinc ion binding
C0015670biological_processcarbon dioxide transport
C0016829molecular_functionlyase activity
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
E0004089molecular_functioncarbonate dehydratase activity
E0006885biological_processregulation of pH
E0008270molecular_functionzinc ion binding
E0015670biological_processcarbon dioxide transport
E0016829molecular_functionlyase activity
E0042597cellular_componentperiplasmic space
E0046872molecular_functionmetal ion binding
G0004089molecular_functioncarbonate dehydratase activity
G0006885biological_processregulation of pH
G0008270molecular_functionzinc ion binding
G0015670biological_processcarbon dioxide transport
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 Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS66
CHIS66
EHIS66
GHIS66

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:9761692
ChainResidueDetails
AHIS92
EHIS94
EHIS111
ETHR177
GHIS92
GHIS94
GHIS111
GTHR177
AHIS94
AHIS111
ATHR177
CHIS92
CHIS94
CHIS111
CTHR177
EHIS92

220113

PDB entries from 2024-05-22

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