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5CXK

Crystal structure of beta carbonic anhydrase from Vibrio cholerae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005737cellular_componentcytoplasm
A0008270molecular_functionzinc ion binding
A0015976biological_processcarbon utilization
A0016829molecular_functionlyase activity
A0034599biological_processcellular response to oxidative stress
A0046872molecular_functionmetal ion binding
A0071244biological_processcellular response to carbon dioxide
B0004089molecular_functioncarbonate dehydratase activity
B0005737cellular_componentcytoplasm
B0008270molecular_functionzinc ion binding
B0015976biological_processcarbon utilization
B0016829molecular_functionlyase activity
B0034599biological_processcellular response to oxidative stress
B0046872molecular_functionmetal ion binding
B0071244biological_processcellular response to carbon dioxide
C0004089molecular_functioncarbonate dehydratase activity
C0005737cellular_componentcytoplasm
C0008270molecular_functionzinc ion binding
C0015976biological_processcarbon utilization
C0016829molecular_functionlyase activity
C0034599biological_processcellular response to oxidative stress
C0046872molecular_functionmetal ion binding
C0071244biological_processcellular response to carbon dioxide
D0004089molecular_functioncarbonate dehydratase activity
D0005737cellular_componentcytoplasm
D0008270molecular_functionzinc ion binding
D0015976biological_processcarbon utilization
D0016829molecular_functionlyase activity
D0034599biological_processcellular response to oxidative stress
D0046872molecular_functionmetal ion binding
D0071244biological_processcellular response to carbon dioxide
E0004089molecular_functioncarbonate dehydratase activity
E0005737cellular_componentcytoplasm
E0008270molecular_functionzinc ion binding
E0015976biological_processcarbon utilization
E0016829molecular_functionlyase activity
E0034599biological_processcellular response to oxidative stress
E0046872molecular_functionmetal ion binding
E0071244biological_processcellular response to carbon dioxide
F0004089molecular_functioncarbonate dehydratase activity
F0005737cellular_componentcytoplasm
F0008270molecular_functionzinc ion binding
F0015976biological_processcarbon utilization
F0016829molecular_functionlyase activity
F0034599biological_processcellular response to oxidative stress
F0046872molecular_functionmetal ion binding
F0071244biological_processcellular response to carbon dioxide
G0004089molecular_functioncarbonate dehydratase activity
G0005737cellular_componentcytoplasm
G0008270molecular_functionzinc ion binding
G0015976biological_processcarbon utilization
G0016829molecular_functionlyase activity
G0034599biological_processcellular response to oxidative stress
G0046872molecular_functionmetal ion binding
G0071244biological_processcellular response to carbon dioxide
H0004089molecular_functioncarbonate dehydratase activity
H0005737cellular_componentcytoplasm
H0008270molecular_functionzinc ion binding
H0015976biological_processcarbon utilization
H0016829molecular_functionlyase activity
H0034599biological_processcellular response to oxidative stress
H0046872molecular_functionmetal ion binding
H0071244biological_processcellular response to carbon dioxide
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
ACYS42
AASP44
AHIS98
ACYS101

site_idAC2
Number of Residues7
Detailsbinding site for residue BCT A 302
ChainResidue
ATYR181
AHOH423
ATRP39
AVAL47
AALA49
AARG64
ACYS96

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BCYS42
BASP44
BHIS98
BCYS101

site_idAC4
Number of Residues9
Detailsbinding site for residue BCT B 302
ChainResidue
BTRP39
BGLY41
BVAL47
BALA49
BLEU52
BARG64
BTYR181
BHOH410
BHOH467

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN H 301
ChainResidue
HCYS42
HASP44
HHIS98
HCYS101

site_idAC6
Number of Residues9
Detailsbinding site for residue BCT H 302
ChainResidue
HTRP39
HGLY41
HVAL47
HPRO48
HALA49
HLEU52
HARG64
HTYR181
HHOH464

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN G 301
ChainResidue
GCYS42
GASP44
GHIS98
GCYS101

site_idAC8
Number of Residues9
Detailsbinding site for residue BCT G 302
ChainResidue
GTRP39
GGLY41
GVAL47
GPRO48
GALA49
GARG64
GTYR181
GHOH438
GHOH444

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DCYS42
DASP44
DHIS98
DCYS101

site_idAD1
Number of Residues8
Detailsbinding site for residue BCT D 302
ChainResidue
DTRP39
DVAL47
DALA49
DLEU52
DARG64
DTYR181
DHOH413
DHOH416

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CCYS42
CASP44
CHIS98
CCYS101

site_idAD3
Number of Residues8
Detailsbinding site for residue BCT C 302
ChainResidue
CTRP39
CGLY41
CVAL47
CALA49
CARG64
CTYR181
CHOH412
CHOH425

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN F 301
ChainResidue
FCYS42
FASP44
FHIS98
FCYS101

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN E 301
ChainResidue
ECYS42
EASP44
EHIS98
ECYS101

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

site_idPS00705
Number of Residues21
DetailsPROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. QYAVdvLqvkhIIVcGHygCG
ChainResidueDetails
AGLN82-GLY102

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PDB entries from 2024-06-12

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