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4WIG

Crystal structure of E47D mutant cytidine deaminase from Mycobacterium tuberculosis (MtCDA E47D)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004126molecular_functioncytidine deaminase activity
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008270molecular_functionzinc ion binding
A0009972biological_processcytidine deamination
A0016787molecular_functionhydrolase activity
A0043100biological_processpyrimidine nucleobase salvage
A0046109biological_processuridine biosynthetic process
A0046872molecular_functionmetal ion binding
A0055086biological_processnucleobase-containing small molecule metabolic process
A0072527biological_processpyrimidine-containing compound metabolic process
A1901135biological_processcarbohydrate derivative metabolic process
B0003824molecular_functioncatalytic activity
B0004126molecular_functioncytidine deaminase activity
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008270molecular_functionzinc ion binding
B0009972biological_processcytidine deamination
B0016787molecular_functionhydrolase activity
B0043100biological_processpyrimidine nucleobase salvage
B0046109biological_processuridine biosynthetic process
B0046872molecular_functionmetal ion binding
B0055086biological_processnucleobase-containing small molecule metabolic process
B0072527biological_processpyrimidine-containing compound metabolic process
B1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 201
ChainResidue
ACYS56
ACYS89
ACYS92
AHOH305

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 201
ChainResidue
BCYS56
BCYS89
BCYS92
BHOH305

Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues41
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. CAEcaVVcalhstgggrllalacvdghgsvlm........PCgr......CrqvL
ChainResidueDetails
ACYS56-LEU96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU58
BGLU58

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN45
BASN45

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20035876, ECO:0007744|PDB:3IJF
ChainResidueDetails
ACYS56
ACYS89
ACYS92
BCYS56
BCYS89
BCYS92

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PDB entries from 2024-11-06

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