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1KOQ

NEISSERIA GONORRHOEAE CARBONIC ANHYDRASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0004089molecular_functioncarbonate dehydratase activity
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS92
AHIS94
AHIS111
AHOH303

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS92
BHIS94
BHIS111
BHOH305

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS66
BHIS66

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:9761692
ChainResidueDetails
AHIS92
AHIS94
AHIS111
ATHR177
BHIS92
BHIS94
BHIS111
BTHR177

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR177
AHIS66

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
BTHR177
BHIS66

227111

PDB entries from 2024-11-06

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