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

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

229380

PDB entries from 2024-12-25

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