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3B1B

The unique structure of wild type carbonic anhydrase alpha-CA1 from Chlamydomonas reinhardtii

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0008270molecular_functionzinc ion binding
B0004089molecular_functioncarbonate dehydratase activity
B0008270molecular_functionzinc ion binding
Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHlLagkiYplELHIV
ChainResidueDetails
ASER168-VAL184

site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. ISFGQWNRYRLAVGL
ChainResidueDetails
AILE279-LEU293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01134
ChainResidueDetails
AHIS112
BHIS112

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01134
ChainResidueDetails
AHIS163
AHIS165
AHIS182
BHIS163
BHIS165
BHIS182

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATHR260
BTHR260

site_idSWS_FT_FI4
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8508810
ChainResidueDetails
AASN101
AASN135
AASN297
BASN101
BASN135
BASN297

224572

PDB entries from 2024-09-04

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