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4CNV

Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0008270molecular_functionzinc ion binding
A0015670biological_processcarbon dioxide transport
A0016829molecular_functionlyase activity
A0018820molecular_functioncyanamide hydratase activity
A0038166biological_processangiotensin-activated signaling pathway
A0044070biological_processregulation of monoatomic anion transport
A0045177cellular_componentapical part of cell
A0046872molecular_functionmetal ion binding
A0051453biological_processregulation of intracellular pH
A2001150biological_processpositive regulation of dipeptide transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 268
ChainResidue
AHIS94
AHIS96
AHIS119
AHOH2110
AHOH2111

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1001
ChainResidue
AHOH2249
AASP32
AASP34
AASP110
AARG111

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 1002
ChainResidue
AASP34
ALYS36

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdrkkYaaELHLV
ChainResidueDetails
ASER105-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15039588","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsSite: {"description":"Fine-tunes the proton-transfer properties of H-64","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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