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1Z93

Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.

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
A0009617biological_processresponse to bacterium
A0016151molecular_functionnickel cation binding
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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 268
ChainResidue
AHIS94
AHIS96
AHIS119
ATHR199
AHOH269

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 Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16042381, ECO:0000269|PubMed:17427958
ChainResidueDetails
ALEU95
ATRP97
ALEU120

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR200

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P07450
ChainResidueDetails
ALYS3

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14141
ChainResidueDetails
APRO30
ALEU44
AVAL49
ATYR51
AALA56
AASP221

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P14141
ChainResidueDetails
ATYR74
APHE131
AVAL218

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P14141
ChainResidueDetails
AASN129

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P16015
ChainResidueDetails
ALYS178

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: S-glutathionyl cysteine => ECO:0000250|UniProtKB:P14141
ChainResidueDetails
ALEU184
AARG189

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR199
ALYS64

236620

PDB entries from 2025-05-28

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