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5JJ4

Crystal Structure of a Variant Human Activation-induced Deoxycytidine Deaminase as an MBP fusion protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008270molecular_functionzinc ion binding
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0034219biological_processcarbohydrate transmembrane transport
A0042597cellular_componentperiplasmic space
A0055085biological_processtransmembrane transport
B0003824molecular_functioncatalytic activity
B0008270molecular_functionzinc ion binding
B0008643biological_processcarbohydrate transport
B0015144molecular_functioncarbohydrate transmembrane transporter activity
B0016787molecular_functionhydrolase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0034219biological_processcarbohydrate transmembrane transport
B0042597cellular_componentperiplasmic space
B0055085biological_processtransmembrane transport
C0003824molecular_functioncatalytic activity
C0008270molecular_functionzinc ion binding
C0008643biological_processcarbohydrate transport
C0015144molecular_functioncarbohydrate transmembrane transporter activity
C0016787molecular_functionhydrolase activity
C0030288cellular_componentouter membrane-bounded periplasmic space
C0034219biological_processcarbohydrate transmembrane transport
C0042597cellular_componentperiplasmic space
C0055085biological_processtransmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues39
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HVEllFLryisdwdldpgrcyrvtwftsws..........PCyd......CarhV
ChainResidueDetails
CHIS1056-VAL1094

site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
CPRO107-ASN124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0ABF6
ChainResidueDetails
CGLU1058
AGLU1058
BGLU1058

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:27258794
ChainResidueDetails
CHIS1056
CCYS1087
CCYS1090
AHIS1056
ACYS1087
ACYS1090
BHIS1056
BCYS1087
BCYS1090

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphothreonine; by PKA => ECO:0000269|PubMed:16387847
ChainResidueDetails
CTHR1027
ATHR1027
BTHR1027

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:16387847, ECO:0000269|PubMed:18722174
ChainResidueDetails
CSER1038
ASER1038
BSER1038

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PDB entries from 2024-07-24

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