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4EG2

2.2 Angstrom Crystal Structure of Cytidine deaminase from Vibrio cholerae in Complex with Zinc and Uridine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004126molecular_functioncytidine deaminase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0009972biological_processcytidine deamination
A0016787molecular_functionhydrolase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0047844molecular_functionobsolete deoxycytidine deaminase activity
B0003824molecular_functioncatalytic activity
B0004126molecular_functioncytidine deaminase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0009972biological_processcytidine deamination
B0016787molecular_functionhydrolase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0047844molecular_functionobsolete deoxycytidine deaminase activity
C0003824molecular_functioncatalytic activity
C0004126molecular_functioncytidine deaminase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0008270molecular_functionzinc ion binding
C0009972biological_processcytidine deamination
C0016787molecular_functionhydrolase activity
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0047844molecular_functionobsolete deoxycytidine deaminase activity
D0003824molecular_functioncatalytic activity
D0004126molecular_functioncytidine deaminase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0008270molecular_functionzinc ion binding
D0009972biological_processcytidine deamination
D0016787molecular_functionhydrolase activity
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0047844molecular_functionobsolete deoxycytidine deaminase activity
E0003824molecular_functioncatalytic activity
E0004126molecular_functioncytidine deaminase activity
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0008270molecular_functionzinc ion binding
E0009972biological_processcytidine deamination
E0016787molecular_functionhydrolase activity
E0042802molecular_functionidentical protein binding
E0046872molecular_functionmetal ion binding
E0047844molecular_functionobsolete deoxycytidine deaminase activity
F0003824molecular_functioncatalytic activity
F0004126molecular_functioncytidine deaminase activity
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0008270molecular_functionzinc ion binding
F0009972biological_processcytidine deamination
F0016787molecular_functionhydrolase activity
F0042802molecular_functionidentical protein binding
F0046872molecular_functionmetal ion binding
F0047844molecular_functionobsolete deoxycytidine deaminase activity
G0003824molecular_functioncatalytic activity
G0004126molecular_functioncytidine deaminase activity
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0008270molecular_functionzinc ion binding
G0009972biological_processcytidine deamination
G0016787molecular_functionhydrolase activity
G0042802molecular_functionidentical protein binding
G0046872molecular_functionmetal ion binding
G0047844molecular_functionobsolete deoxycytidine deaminase activity
H0003824molecular_functioncatalytic activity
H0004126molecular_functioncytidine deaminase activity
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0008270molecular_functionzinc ion binding
H0009972biological_processcytidine deamination
H0016787molecular_functionhydrolase activity
H0042802molecular_functionidentical protein binding
H0046872molecular_functionmetal ion binding
H0047844molecular_functionobsolete deoxycytidine deaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS102
ACYS129
ACYS132
AURI302

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE URI A 302
ChainResidue
AVAL101
AHIS102
AALA103
AGLU104
APRO128
ACYS129
AZN301
AHOH514
BALA232
APHE71
AVAL73
AASN89
AGLU91
ATHR100

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 303
ChainResidue
AGLU253
APHE255

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BHOH499
BHOH604
BHOH605
EHOH551
EHOH552
FHOH559

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS102
BCYS129
BCYS132
BURI303

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE URI B 303
ChainResidue
AALA232
AALA233
BPHE71
BVAL73
BASN89
BGLU91
BTHR100
BVAL101
BHIS102
BALA103
BGLU104
BPRO128
BCYS129
BZN302

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 304
ChainResidue
BTYR65
BGLU253
BPHE255

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 301
ChainResidue
CHIS102
CCYS129
CCYS132
CURI302

site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE URI C 302
ChainResidue
CPHE71
CASN89
CGLU91
CTHR100
CVAL101
CHIS102
CALA103
CGLU104
CPRO128
CCYS129
CZN301
DALA232
DALA233

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
DHIS102
DCYS129
DCYS132
DURI302

site_idBC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE URI D 302
ChainResidue
CPHE165
CALA232
CALA233
CPHE234
DPHE71
DVAL73
DASN89
DGLU91
DTHR100
DVAL101
DHIS102
DALA103
DGLU104
DPRO128
DCYS129
DZN301

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT D 303
ChainResidue
BARG198
DGLN40

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT D 304
ChainResidue
DTYR65
DGLU253
DPHE255

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 301
ChainResidue
EHIS102
ECYS129
ECYS132
EURI302

site_idBC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE URI E 302
ChainResidue
EALA103
EGLU104
EPRO128
ECYS129
EZN301
FALA232
FALA233
FPHE234
EPHE71
EVAL73
EASN89
EGLU91
ETHR100
EHIS102

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT E 303
ChainResidue
EGLU253
EPHE255

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT E 304
ChainResidue
EARG4
EALA66
EGLU70
ETYR72

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT E 305
ChainResidue
EASP51
ELYS151
EARG152

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 301
ChainResidue
FHIS102
FCYS129
FCYS132
FURI302

site_idCC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE URI F 302
ChainResidue
EALA232
EALA233
FPHE71
FVAL73
FASN89
FGLU91
FTHR100
FVAL101
FHIS102
FALA103
FGLU104
FPRO128
FCYS129
FZN301

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT F 303
ChainResidue
FTYR65
FGLU253
FPHE255

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G 301
ChainResidue
GHIS102
GCYS129
GCYS132
GURI302

site_idCC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE URI G 302
ChainResidue
GPHE71
GVAL73
GASN89
GGLU91
GTHR100
GVAL101
GHIS102
GALA103
GGLU104
GSER127
GPRO128
GCYS129
GZN301
HALA232
HALA233
HPHE234

site_idCC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT G 303
ChainResidue
GGLU253
GPHE255

site_idCC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 301
ChainResidue
HHIS102
HCYS129
HCYS132
HURI302

site_idCC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE URI H 302
ChainResidue
GALA232
GPHE234
HASN89
HGLU91
HTHR100
HVAL101
HHIS102
HALA103
HGLU104
HPRO128
HCYS129
HZN301

Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues35
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAEqcAIshawmkgekgvaditinfs..............PCgh......CrqfM
ChainResidueDetails
AHIS102-MSE136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01558
ChainResidueDetails
AGLU104
BGLU104
CGLU104
DGLU104
EGLU104
FGLU104
GGLU104
HGLU104

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01558
ChainResidueDetails
GASN89
GHIS102
GCYS129
GCYS132
HASN89
HHIS102
HCYS129
HCYS132
ECYS129
ECYS132
FASN89
FHIS102
FCYS129
FCYS132
AASN89
AHIS102
ACYS129
ACYS132
BASN89
BHIS102
BCYS129
BCYS132
CASN89
CHIS102
CCYS129
CCYS132
DASN89
DHIS102
DCYS129
DCYS132
EASN89
EHIS102

221051

PDB entries from 2024-06-12

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