Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3UYN

HCA 3

Replaces:  2HFY
Functional Information from GO Data
ChainGOidnamespacecontents
A0003009biological_processskeletal muscle contraction
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0008270molecular_functionzinc ion binding
A0008284biological_processpositive regulation of cell population proliferation
A0016791molecular_functionphosphatase activity
A0016829molecular_functionlyase activity
A0030017cellular_componentsarcomere
A0032869biological_processcellular response to insulin stimulus
A0033993biological_processresponse to lipid
A0043066biological_processnegative regulation of apoptotic process
A0044320biological_processcellular response to leptin stimulus
A0045471biological_processresponse to ethanol
A0046872molecular_functionmetal ion binding
A0071456biological_processcellular response to hypoxia
A0097305biological_processresponse to alcohol
A0097421biological_processliver regeneration
A1903427biological_processnegative regulation of reactive oxygen species biosynthetic process
A1903751biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 262
ChainResidue
AHIS94
AHIS96
AHIS119
AHOH360

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdgvkYaaELHLV
ChainResidueDetails
ASER105-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues256
DetailsDomain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsRegion: {"description":"Involved in proton transfer","evidences":[{"source":"PubMed","id":"17427958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16042381","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17427958","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P07450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14141","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P14141","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14141","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P16015","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"S-glutathionyl cysteine","evidences":[{"source":"UniProtKB","id":"P14141","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon