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1VQ2

CRYSTAL STRUCTURE OF T4-BACTERIOPHAGE DEOXYCYTIDYLATE DEAMINASE, MUTANT R115E

Replaces:  1TEO
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004132molecular_functiondCMP deaminase activity
A0005737cellular_componentcytoplasm
A0006220biological_processpyrimidine nucleotide metabolic process
A0008270molecular_functionzinc ion binding
A0009165biological_processnucleotide biosynthetic process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 701
ChainResidue
AHIS104
ACYS132
ACYS135
ADDN308

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 702
ChainResidue
ACYS19
ACYS49
AHIS94
AGLU102

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE DDN A 308
ChainResidue
ASER21
ATRP22
AVAL24
AASN40
AARG91
AHIS94
ASER95
ASER98
AGLU102
AHIS104
AALA105
AGLU106
APRO131
ACYS132
ACYS135
ATYR153
ALYS155
AZN701
ACYS19

Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues36
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAElnAIlfaaengssiegatmyvtls.............PCpd......CakaI
ChainResidueDetails
AHIS104-ILE139

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU106

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ACYS19
ACYS49
AHIS94
AGLU102
AHIS104
ACYS132
ACYS135
ATYR153

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PDB entries from 2024-06-12

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