Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1CTT

TRANSITION-STATE SELECTIVITY FOR A SINGLE OH GROUP DURING CATALYSIS BY CYTIDINE DEAMINASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0001884molecular_functionpyrimidine nucleoside binding
A0003824molecular_functioncatalytic activity
A0004126molecular_functioncytidine deaminase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006217biological_processdeoxycytidine catabolic process
A0008270molecular_functionzinc ion binding
A0009972biological_processcytidine deamination
A0015949biological_processnucleobase-containing small molecule interconversion
A0016787molecular_functionhydrolase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0047844molecular_functionobsolete deoxycytidine deaminase activity
Functional Information from PDB Data
site_idA1
Number of Residues4
DetailsCATALYTIC SITE IN WHICH A ZINC IS COORDINATED IN A TETRAHEDRAL LIGAND FIELD
ChainResidue
AHIS102
AGLU104
ACYS129
ACYS132

site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 296
ChainResidue
AHIS102
AGLU104
ACYS129
ACYS132
AHOH700

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DHZ A 295
ChainResidue
APHE71
AVAL73
AASN89
AGLU91
ATHR100
AVAL101
AHIS102
AALA103
AGLU104
AALA231
APHE233
AHOH700

Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues35
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAEqsAIshawlsgekalaaitvnyt..............PCgh......CrqfM
ChainResidueDetails
AHIS102-MET136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:8289286, ECO:0000305|PubMed:8634261, ECO:0000305|PubMed:9125497
ChainResidueDetails
AGLU104

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:8289286, ECO:0000305|PubMed:8634261, ECO:0000305|PubMed:9125497
ChainResidueDetails
ACYS132
AASN89
AHIS102
ACYS129

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 97
ChainResidueDetails
AHIS102metal ligand
AGLU104electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ACYS129metal ligand
ACYS132metal ligand

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon