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4X5S

The crystal structure of an alpha carbonic anhydrase from the extremophilic bacterium Sulfurihydrogenibium azorense.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0046872molecular_functionmetal ion binding
B0004089molecular_functioncarbonate dehydratase activity
B0006730biological_processone-carbon metabolic process
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS89
AHIS91
AHIS108
AAZM302

site_idAC2
Number of Residues12
Detailsbinding site for residue AZM A 302
ChainResidue
ALEU173
ATHR174
ATHR175
ATRP184
AZN301
APE8303
AHOH474
AGLN87
AHIS89
AHIS91
AHIS108
AVAL110

site_idAC3
Number of Residues11
Detailsbinding site for residue PE8 A 303
ChainResidue
AVAL70
AGLU72
AASP73
AHIS84
ALEU85
ALYS86
ALYS112
AASP113
AILE118
AAZM302
AHOH512

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS89
BHIS91
BHIS108
BAZM302

site_idAC5
Number of Residues12
Detailsbinding site for residue AZM B 302
ChainResidue
BGLN87
BHIS89
BHIS91
BHIS108
BVAL110
BLEU173
BTHR174
BTHR175
BTRP184
BZN301
BPE8303
BHOH519

site_idAC6
Number of Residues9
Detailsbinding site for residue PE8 B 303
ChainResidue
BVAL70
BGLU72
BASP73
BHIS84
BLYS86
BLYS112
BASP113
BILE118
BAZM302

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVngkyYplEMHLV
ChainResidueDetails
ASER94-VAL110

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PDB entries from 2024-07-24

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