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2A8D

Haemophilus influenzae beta-carbonic anhydrase complexed with bicarbonate

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
C0004089molecular_functioncarbonate dehydratase activity
C0008270molecular_functionzinc ion binding
C0015976biological_processcarbon utilization
C0016829molecular_functionlyase activity
C0046872molecular_functionmetal ion binding
D0004089molecular_functioncarbonate dehydratase activity
D0008270molecular_functionzinc ion binding
D0015976biological_processcarbon utilization
D0016829molecular_functionlyase activity
D0046872molecular_functionmetal ion binding
E0004089molecular_functioncarbonate dehydratase activity
E0008270molecular_functionzinc ion binding
E0015976biological_processcarbon utilization
E0016829molecular_functionlyase activity
E0046872molecular_functionmetal ion binding
F0004089molecular_functioncarbonate dehydratase activity
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 ZN A 1230
ChainResidue
ACYS42
AASP44
AHIS98
ACYS101

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2230
ChainResidue
BCYS42
BASP44
BHIS98
BCYS101

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 3230
ChainResidue
CASP44
CHIS98
CCYS101
CCYS42

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 4230
ChainResidue
DCYS42
DASP44
DHIS98
DCYS101

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 5230
ChainResidue
ECYS42
EASP44
EHIS98
ECYS101

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 6230
ChainResidue
FCYS42
FASP44
FHIS98
FCYS101

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCT A 1001
ChainResidue
ATRP39
AGLY41
AVAL47
APRO48
AALA49
AARG64
ATYR181
AHOH1233
AHOH1239

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCT B 1002
ChainResidue
BTRP39
BGLY41
BVAL47
BALA49
BLEU52
BARG64
BTYR181
BHOH2247
BHOH2248

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCT C 1003
ChainResidue
CTRP39
CGLY41
CVAL47
CALA49
CLEU52
CARG64
CTYR181
CHOH3233
CHOH3242

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCT D 1004
ChainResidue
DTRP39
DGLY41
DVAL47
DPRO48
DALA49
DARG64
DTYR181
DHOH4233
DHOH4236

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCT E 1005
ChainResidue
ETRP39
EGLY41
EVAL47
EPRO48
EALA49
EARG64
ETYR181
EHOH5244
EHOH5261

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BCT F 1006
ChainResidue
FTRP39
FVAL47
FALA49
FARG64
FTYR181
FHOH6233
FHOH6234

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 2001
ChainResidue
AARG160
ALYS165
AARG198
BLEU121
BARG124

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 2002
ChainResidue
AARG124
APHE128
BARG160
BARG198
BHOH2243

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 2003
ChainResidue
CARG160
CARG198
CHOH3240
DARG124

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 2004
ChainResidue
CARG124
DARG160
DARG198
DHOH4245

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 E 2005
ChainResidue
EARG160
ELYS165
EARG198
EHOH5236
FARG124

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 E 2006
ChainResidue
ELEU121
EARG124
EPHE128
EHOH5237
FARG160
FARG198

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 site: {"evidences":[{"source":"PubMed","id":"16584170","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A8D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i6p
ChainResidueDetails
AASP44
AARG46

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i6p
ChainResidueDetails
BASP44
BARG46

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i6p
ChainResidueDetails
CASP44
CARG46

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i6p
ChainResidueDetails
DASP44
DARG46

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i6p
ChainResidueDetails
EASP44
EARG46

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i6p
ChainResidueDetails
FASP44
FARG46

239803

PDB entries from 2025-08-06

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