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8YGC

The Dimer Structure of DSR2-SPR

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0051607biological_processdefense response to virus
B0016787molecular_functionhydrolase activity
B0051607biological_processdefense response to virus
E0016787molecular_functionhydrolase activity
E0051607biological_processdefense response to virus
F0016787molecular_functionhydrolase activity
F0051607biological_processdefense response to virus
Functional Information from PROSITE/UniProt
site_idPS00216
Number of Residues17
DetailsSUGAR_TRANSPORT_1 Sugar transport proteins signature 1. AVYQIEKVGRRlaika.S
ChainResidueDetails
CALA149-SER165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:39039073, ECO:0000305|PubMed:39059542
ChainResidueDetails
ATYR134
FTYR134
FASP135
FALA171
AASP135
AALA171
BTYR134
BASP135
BALA171
ETYR134
EASP135
EALA171

site_idSWS_FT_FI2
Number of Residues40
DetailsSITE: Interaction with the phage SPR tail tube monomeric protein => ECO:0000269|PubMed:38729958
ChainResidueDetails
ALYS31
ALEU498
BLYS31
BGLU32
BVAL50
BSER51
BTHR52
BMET204
BTHR206
BLEU495
BLEU497
AGLU32
BLEU498
ELYS31
EGLU32
EVAL50
ESER51
ETHR52
EMET204
ETHR206
ELEU495
ELEU497
AVAL50
ELEU498
FLYS31
FGLU32
FVAL50
FSER51
FTHR52
FMET204
FTHR206
FLEU495
FLEU497
ASER51
FLEU498
ATHR52
AMET204
ATHR206
ALEU495
ALEU497

site_idSWS_FT_FI3
Number of Residues28
DetailsSITE: Interaction with phage SPR tail tube monomeric protein => ECO:0000269|PubMed:38729958
ChainResidueDetails
ATYR574
BILE918
BTRP919
BLEU922
BTYR962
BLEU966
ETYR574
EPHE576
EILE918
ETRP919
ELEU922
APHE576
ETYR962
ELEU966
FTYR574
FPHE576
FILE918
FTRP919
FLEU922
FTYR962
FLEU966
AILE918
ATRP919
ALEU922
ATYR962
ALEU966
BTYR574
BPHE576

237735

PDB entries from 2025-06-18

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