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3E1V

H. influenzae beta-carbonic anhydrase, variant D44N

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0008270molecular_functionzinc ion binding
A0015976biological_processcarbon utilization
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0004089molecular_functioncarbonate dehydratase activity
B0008270molecular_functionzinc ion binding
B0015976biological_processcarbon utilization
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 230
ChainResidue
ACYS42
AASN44
AHIS98
ACYS101
AHOH231

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 230
ChainResidue
BHOH231
BCYS42
BASN44
BHIS98
BCYS101

Functional Information from PROSITE/UniProt
site_idPS00705
Number of Residues21
DetailsPROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. QYAVdvLkiehIIIcGHtnCG
ChainResidueDetails
AGLN82-GLY102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16584170, ECO:0007744|PDB:2A8C, ECO:0007744|PDB:2A8D
ChainResidueDetails
ACYS42
AASN44
AHIS98
ACYS101
BCYS42
BASN44
BHIS98
BCYS101

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i6p
ChainResidueDetails
AASN44
AARG46

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i6p
ChainResidueDetails
BASN44
BARG46

237735

PDB entries from 2025-06-18

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