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5SWC

The structure of the beta-carbonic anhydrase CcaA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0008270molecular_functionzinc ion binding
A0015976biological_processcarbon utilization
B0004089molecular_functioncarbonate dehydratase activity
B0008270molecular_functionzinc ion binding
B0015976biological_processcarbon utilization
C0004089molecular_functioncarbonate dehydratase activity
C0008270molecular_functionzinc ion binding
C0015976biological_processcarbon utilization
D0004089molecular_functioncarbonate dehydratase activity
D0008270molecular_functionzinc ion binding
D0015976biological_processcarbon utilization
E0004089molecular_functioncarbonate dehydratase activity
E0008270molecular_functionzinc ion binding
E0015976biological_processcarbon utilization
F0004089molecular_functioncarbonate dehydratase activity
F0008270molecular_functionzinc ion binding
F0015976biological_processcarbon utilization
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 301
ChainResidue
ACYS39
AHIS98
ACYS101
BFMT303
BHOH422

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 302
ChainResidue
AHOH526
ALYS160
AGLN163
AGLU212
AHOH448

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 303
ChainResidue
AARG61
BARG61

site_idAC4
Number of Residues8
Detailsbinding site for residue FMT A 304
ChainResidue
AGLN30
APHE58
ATYR83
AHOH417
AHOH551
BCYS39
BALA103
BZN301

site_idAC5
Number of Residues6
Detailsbinding site for residue FMT A 305
ChainResidue
AGLU82
ATYR165
APRO166
AALA167
AHOH468
AHOH542

site_idAC6
Number of Residues7
Detailsbinding site for residue FMT A 306
ChainResidue
AHIS180
ATRP182
AALA193
APRO204
AGLN205
AILE208
AHOH466

site_idAC7
Number of Residues5
Detailsbinding site for residue ZN B 301
ChainResidue
AFMT304
AHOH417
BCYS39
BHIS98
BCYS101

site_idAC8
Number of Residues5
Detailsbinding site for residue FMT B 302
ChainResidue
BGLU82
BTYR165
BPRO166
BALA167
BHOH419

site_idAC9
Number of Residues7
Detailsbinding site for residue FMT B 303
ChainResidue
AALA103
AZN301
BGLN30
BPHE58
BTYR83
BHOH422
BHOH553

site_idAD1
Number of Residues7
Detailsbinding site for residue FMT B 304
ChainResidue
BHIS180
BTRP182
BALA193
BPRO204
BGLN205
BILE208
BHOH476

site_idAD2
Number of Residues7
Detailsbinding site for residue FMT B 305
ChainResidue
ASER27
AHIS28
AGLY29
BARG43
BHIS100
BLYS105
BHOH545

site_idAD3
Number of Residues7
Detailsbinding site for residue FMT B 306
ChainResidue
ASER18
AHIS19
AARG20
AASP21
ALEU22
BARG33
BHOH488

site_idAD4
Number of Residues5
Detailsbinding site for residue ZN C 301
ChainResidue
CCYS39
CHIS98
CCYS101
CFMT304
CHOH406

site_idAD5
Number of Residues3
Detailsbinding site for residue CL C 302
ChainResidue
CARG61
DARG61
DHOH505

site_idAD6
Number of Residues7
Detailsbinding site for residue FMT C 303
ChainResidue
CGLN30
CPHE58
CTYR83
CHOH409
CHOH477
DALA103
DZN301

site_idAD7
Number of Residues7
Detailsbinding site for residue FMT C 304
ChainResidue
CCYS39
CALA103
CZN301
CHOH406
CHOH507
DGLN30
DTYR83

site_idAD8
Number of Residues5
Detailsbinding site for residue FMT C 305
ChainResidue
CGLU82
CTYR165
CPRO166
CALA167
CHOH433

site_idAD9
Number of Residues5
Detailsbinding site for residue FMT C 306
ChainResidue
CGLY29
DARG43
DHIS100
DLYS105
CHIS28

site_idAE1
Number of Residues5
Detailsbinding site for residue ZN D 301
ChainResidue
CFMT303
CHOH409
DCYS39
DHIS98
DCYS101

site_idAE2
Number of Residues6
Detailsbinding site for residue FMT D 302
ChainResidue
DGLU82
DTYR165
DPRO166
DALA167
DHOH461
DHOH504

site_idAE3
Number of Residues5
Detailsbinding site for residue FMT D 303
ChainResidue
CMET1
DHIS180
DTRP182
DALA193
DHOH422

site_idAE4
Number of Residues5
Detailsbinding site for residue ZN E 301
ChainResidue
ECYS39
EHIS98
ECYS101
EFMT305
EHOH411

site_idAE5
Number of Residues4
Detailsbinding site for residue CL E 302
ChainResidue
ELYS160
EGLN163
EGLU212
EHOH474

site_idAE6
Number of Residues2
Detailsbinding site for residue CL E 303
ChainResidue
EARG61
FARG61

site_idAE7
Number of Residues6
Detailsbinding site for residue FMT E 304
ChainResidue
EGLU82
ETYR165
EPRO166
EALA167
EHOH480
EHOH514

site_idAE8
Number of Residues7
Detailsbinding site for residue FMT E 305
ChainResidue
ECYS39
EALA103
EZN301
EHOH411
FGLN30
FPHE58
FTYR83

site_idAE9
Number of Residues8
Detailsbinding site for residue FMT E 306
ChainResidue
EGLN30
EPHE58
ETYR83
EHOH410
EHOH521
FCYS39
FALA103
FZN301

site_idAF1
Number of Residues6
Detailsbinding site for residue FMT E 307
ChainResidue
EARG43
EHIS100
ELYS105
FSER27
FHIS28
FGLY29

site_idAF2
Number of Residues7
Detailsbinding site for residue FMT E 308
ChainResidue
EHIS180
ETRP182
EALA193
EPRO204
EGLN205
EILE208
EHOH470

site_idAF3
Number of Residues5
Detailsbinding site for residue ZN F 301
ChainResidue
EFMT306
EHOH410
FCYS39
FHIS98
FCYS101

site_idAF4
Number of Residues6
Detailsbinding site for residue FMT F 302
ChainResidue
FGLU82
FTYR165
FPRO166
FALA167
FHOH430
FHOH521

site_idAF5
Number of Residues6
Detailsbinding site for residue FMT F 303
ChainResidue
ESER27
EHIS28
EGLY29
FARG43
FHIS100
FLYS105

Functional Information from PROSITE/UniProt
site_idPS00704
Number of Residues8
DetailsPROK_CO2_ANHYDRASE_1 Prokaryotic-type carbonic anhydrases signature 1. CSDSRVdP
ChainResidueDetails
ACYS39-PRO46

site_idPS00705
Number of Residues21
DetailsPROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. EYALvaLeinqIIVcGHshCG
ChainResidueDetails
AGLU82-GLY102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:27729545, ECO:0007744|PDB:5SWC
ChainResidueDetails
ACYS39
DCYS39
DHIS98
DCYS101
ECYS39
EHIS98
ECYS101
FCYS39
FHIS98
FCYS101
AHIS98
ACYS101
BCYS39
BHIS98
BCYS101
CCYS39
CHIS98
CCYS101

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PDB entries from 2025-06-11

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