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3EYX

Crystal structure of Carbonic Anhydrase Nce103 from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0008270molecular_functionzinc ion binding
A0015976biological_processcarbon utilization
A0016829molecular_functionlyase activity
A0034599biological_processcellular response to oxidative stress
A0046872molecular_functionmetal ion binding
A0071244biological_processcellular response to carbon dioxide
B0004089molecular_functioncarbonate dehydratase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005758cellular_componentmitochondrial intermembrane space
B0008270molecular_functionzinc ion binding
B0015976biological_processcarbon utilization
B0016829molecular_functionlyase activity
B0034599biological_processcellular response to oxidative stress
B0046872molecular_functionmetal ion binding
B0071244biological_processcellular response to carbon dioxide
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
ACYS57
AHIS112
ACYS115
AACT222
AHOH263

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ACT A 222
ChainResidue
ACYS115
AGLY116
AGLY117
AHOH257
AHOH263
BPHE75
BPHE97
AZN1
ACYS57
AVAL80
AALA81

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ACT A 2
ChainResidue
APHE75
APHE97
AHOH299
AHOH300
BZN2
BCYS57
BVAL80
BALA81
BCYS115
BGLY116
BGLY117

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 3
ChainResidue
AHIS85
ASER86
AARG179
AHOH289

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 4
ChainResidue
APRO184
ATHR188
AHOH275
AHOH277
BGLU87

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 2
ChainResidue
AACT2
AHOH300
BCYS57
BHIS112
BCYS115

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1
ChainResidue
BHIS85
BSER86
BARG179
BHOH264
BHOH292

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 222
ChainResidue
BTHR113
BHIS166
BASN203
BGLU205
BHOH269
BHOH293

Functional Information from PROSITE/UniProt
site_idPS00705
Number of Residues21
DetailsPROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. EFAIicLkvnkVIIcGHtdCG
ChainResidueDetails
AGLU96-GLY116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19852838, ECO:0007744|PDB:3EYX
ChainResidueDetails
ACYS57
AHIS112
ACYS115
BCYS57
BHIS112
BCYS115

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P61517
ChainResidueDetails
AASP59
BASP59

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i6p
ChainResidueDetails
AARG61
AASP59

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i6p
ChainResidueDetails
BARG61
BASP59

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PDB entries from 2024-07-24

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