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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
A0006730biological_processone-carbon metabolic process
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
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS64

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15039588
ChainResidueDetails
AHIS94
AHIS96
AHIS119

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR198

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATYR7
AASN62
AASN67

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139
ChainResidueDetails
ASER2

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ASER165
ASER172

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PDB entries from 2024-07-24

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