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3MF3

Cobalt(II)-Substituted Haemophilus influenzae B-Carbonic Anhydrase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005575cellular_componentcellular_component
A0008270molecular_functionzinc ion binding
A0015976biological_processcarbon utilization
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0004089molecular_functioncarbonate dehydratase activity
B0005575cellular_componentcellular_component
B0008270molecular_functionzinc ion binding
B0015976biological_processcarbon utilization
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
C0004089molecular_functioncarbonate dehydratase activity
C0005575cellular_componentcellular_component
C0008270molecular_functionzinc ion binding
C0015976biological_processcarbon utilization
C0016829molecular_functionlyase activity
C0046872molecular_functionmetal ion binding
D0004089molecular_functioncarbonate dehydratase activity
D0005575cellular_componentcellular_component
D0008270molecular_functionzinc ion binding
D0015976biological_processcarbon utilization
D0016829molecular_functionlyase activity
D0046872molecular_functionmetal ion binding
E0004089molecular_functioncarbonate dehydratase activity
E0005575cellular_componentcellular_component
E0008270molecular_functionzinc ion binding
E0015976biological_processcarbon utilization
E0016829molecular_functionlyase activity
E0046872molecular_functionmetal ion binding
F0004089molecular_functioncarbonate dehydratase activity
F0005575cellular_componentcellular_component
F0008270molecular_functionzinc ion binding
F0015976biological_processcarbon utilization
F0016829molecular_functionlyase activity
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 230
ChainResidue
ACYS42
AASP44
AHIS98
ACYS101

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO B 230
ChainResidue
BCYS42
BASP44
BHIS98
BCYS101

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO C 230
ChainResidue
CASP44
CHIS98
CCYS101
CCYS42

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO D 230
ChainResidue
DCYS42
DASP44
DHIS98
DCYS101

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO E 230
ChainResidue
ECYS42
EASP44
EHIS98
ECYS101

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO F 230
ChainResidue
FCYS42
FASP44
FHIS98
FCYS101

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ACT E 222
ChainResidue
CTHR73
CASP74
CPHE75
DACT222
DHOH238
ETHR73
EASP74
EPHE75
EASN76
EHOH246

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT D 222
ChainResidue
DTHR73
DASP74
DPHE75
EACT222
EHOH246
FTHR73
FASP74
FPHE75

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ACT B 222
ChainResidue
AACT222
AACT222
AHOH250
AHOH250
BTHR73
BTHR73
BASP74
BASP74
BPHE75
BPHE75
BASN76

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ACT A 222
ChainResidue
ATHR73
ATHR73
AASP74
AASP74
APHE75
APHE75
AHOH250
AHOH250
BACT222
BACT222
BHOH229

Functional Information from PROSITE/UniProt
site_idPS00704
Number of Residues8
DetailsPROK_CO2_ANHYDRASE_1 Prokaryotic-type carbonic anhydrases signature 1. CSDSRVpA
ChainResidueDetails
ACYS42-ALA49

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 Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:16584170, ECO:0007744|PDB:2A8C, ECO:0007744|PDB:2A8D
ChainResidueDetails
ACYS42
AASP44
EHIS98
ECYS101
FCYS42
FASP44
FHIS98
FCYS101
AHIS98
ACYS101
BCYS42
BASP44
BHIS98
BCYS101
CCYS42
CASP44
CHIS98
CCYS101
DCYS42
DASP44
DHIS98
DCYS101
ECYS42
EASP44

219869

PDB entries from 2024-05-15

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