eF-site ID 4puf-ABCD PDB Code 4puf Chain A, B, C, D click to enlarge Title Complex between the Salmonella T3SS effector SlrP and its human target thioredoxin-1 Classification LIGASE/OXIDOREDUCTASE Compound E3 ubiquitin-protein ligase SlrP Source null (THIO_HUMAN) Sequence A:  ELIWSEWVKEAPAKEAANREEAVQRMRDCLKNNKTELRLK ILGLTTIPAYIPEQITTLILDNNELKSLPENLQGNIKTLY ANSNQLTSIPATLPDTIQEMELSINRITELPERLPSALQS LDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSEI THLNVQSNSLTALPETLPPGLKTLEAGENALTSLPASLPP ELQVLDVSKNQITVLPETLPPTITTLDVSRNALTNLPENL PAALQIMQASRNNLVRLPESLPHFRGEGPQPTRIIVEYNP FSERTIQNMQRLMSSVDYQGPRVLFAMGDFSIVRVTRPLH QAVQGWLTSLEEEDVNQWRAFEAEANAAAFSGFLDYLGDT QNTRHPDFKEQVSAWLMRLAEDSALRETVFIIAMNATISC EDRVTLAYHQMQEATLVHDAERGAFDSHLAELIMAGREIF RLEQIESLAREKVKRLFFIDEVEVFLGFQNQLRESLSLTT MTRDMRFYNVSGITESDLDEAEIRIKMAENRDFHKWFALW GPWHKVLERIAPEEWREMMAKRDECIETDEYQSRVNAELE DLRAIGIKIMEEINQTLFTEIMENILLKKEVSSLMSAYW B:  ELIWSEWVKEAPAKEAANREEAVQRMRDCLKNNKTELRLK ILGLTTIPAYIPEQITTLILDNNELKSLPENLQGNIKTLY ANSNQLTSIPATLPDTIQEMELSINRITELPERLPSALQS LDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSEI THLNVQSNSLTALPETLPPGLKTLEAGENALTSLPASLPP ELQVLDVSKNQITVLPETLPPTITTLDVSRNALTNLPENL PAALQIMQASRNNLVRLPESLPHFRGEGPQPTRIIVEYNP FSERTIQNMQRLMSSVDYQGPRVLFAMGDFSIVRVTRPLH QAVQGWLTSLEEEDVNQWRAFEAEANAAAFSGFLDYLGDT QNTRHPDFKEQVSAWLMRLAEDSALRETVFIIAMNATISC EDRVTLAYHQMQEATLVHDAERGAFDSHLAELIMAGREIF RLEQIESLAREKVKRLFFIDEVEVFLGFQNQLRESLSLTT MTRDMRFYNVSGITESDLDEAEIRIKMAENRDFHKWFALW GPWHKVLERIAPEEWREMMAKRDECIETDEYQSRVNAELE DAIGIKIMEEINQTLFTEIMENILLKKEVSSLMSAYWR C:  HHHHHGSMVKQIESKTAFQEALDAAGDKLVVVDFSATWCG PCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKC MPTFQFFKKGQKVGEFSGANKEKLEATINELV D:  HHHHHGSMVKQIESKTAFQEALDAAGDKLVVVDFSATWCG PCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKC MPTFQFFKKGQKVGEFSGANKEKLEATINELV Description Functional site 1) chain C residue 24-42 type prosite sequence VVDFSATWCGPCKMIKPFF description THIOREDOXIN_1 Thioredoxin family active site. VVdFSatWCGPCKmIkpfF source prosite : PS00194 2) chain C residue 32 type ACT_SITE sequence C description Nucleophile => ECO:0000269|PubMed:9108029 source Swiss-Prot : SWS_FT_FI1 3) chain C residue 35 type ACT_SITE sequence C description Nucleophile => ECO:0000269|PubMed:9108029 source Swiss-Prot : SWS_FT_FI1 4) chain D residue 32 type ACT_SITE sequence C description Nucleophile => ECO:0000269|PubMed:9108029 source Swiss-Prot : SWS_FT_FI1 5) chain D residue 35 type ACT_SITE sequence C description Nucleophile => ECO:0000269|PubMed:9108029 source Swiss-Prot : SWS_FT_FI1 6) chain C residue 26 type SITE sequence D description Deprotonates C-terminal active site Cys => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 7) chain D residue 26 type SITE sequence D description Deprotonates C-terminal active site Cys => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 8) chain C residue 33 type SITE sequence G description Contributes to redox potential value => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 9) chain C residue 34 type SITE sequence P description Contributes to redox potential value => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 10) chain D residue 33 type SITE sequence G description Contributes to redox potential value => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 11) chain D residue 34 type SITE sequence P description Contributes to redox potential value => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 12) chain C residue 3 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 13) chain C residue 39 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 14) chain D residue 3 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 15) chain D residue 39 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 16) chain C residue 8 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P10639 source Swiss-Prot : SWS_FT_FI5 17) chain D residue 8 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P10639 source Swiss-Prot : SWS_FT_FI5 18) chain C residue 62 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:17260951 source Swiss-Prot : SWS_FT_FI6 19) chain C residue 69 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:17260951 source Swiss-Prot : SWS_FT_FI6 20) chain D residue 62 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:17260951 source Swiss-Prot : SWS_FT_FI6 21) chain D residue 69 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:17260951 source Swiss-Prot : SWS_FT_FI6 22) chain C residue 73 type MOD_RES sequence C description S-nitrosocysteine; alternate => ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17606900 source Swiss-Prot : SWS_FT_FI7 23) chain D residue 73 type MOD_RES sequence C description S-nitrosocysteine; alternate => ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17606900 source Swiss-Prot : SWS_FT_FI7 24) chain C residue 94 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P10639 source Swiss-Prot : SWS_FT_FI8 25) chain D residue 94 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P10639 source Swiss-Prot : SWS_FT_FI8

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