eF-site ID 2b5u-ABCD PDB Code 2b5u Chain A, B, C, D click to enlarge Title Crystal Structure Of Colicin E3 V206C Mutant In Complex With Its Immunity Protein Classification RIBOSOME INHIBITOR, HYDROLASE Compound Colicin E3 Source Escherichia coli (IMM3_ECOLI) Sequence A:  SAVAAPVAFGFPALSTPGAGGLAVSISAGALSAAIADIMA ALKGPFKFGLWGVALYGVLPSQIAKDDPNMMSKIVTSLPA DDITESPVSSLPLDKATVNVNVRVVDDVKDERQNISVVSG VPMSCPVVDAKPTERPGVFTASIPGAPVLNISVNNSTPAV QTLSPGVTNNTDKDVRPAGFTQGGNTRDAVIRFPKDSGHN AVYVSVSDVLSPDQVKQRQDEENRRQQEWDATHPVEAAER NYERARAELNQANEDVARNQERQAKAVQVYNSRKSELDAA NKTLADAIAEIKQFNRFAHDPMAGGHRMWQMAGLKAQRAQ TDVNNKQAAFDAAAKEKSDADAALSSAMESRKKKEDKKRS AENNLNDEKNKPRKGFKDYGHDYHPAPKTENIKGLGDLKP GIPKTPKQNGGGKRKRWTGDKGRKIYEWDSQHGELEGYRA SDGQHLGSFDPKTGNQLKGPDPKRNIKKYL B:  GLKLDLTWFDKSTEDFKGEEYSKDFGDDGSVMESLGVPFK DNVNNGCFDVIAEWVPLLQPYFNHQIDISDNEYFVSFDYR DGDW C:  SAVAAPVAFGFPALSTPGAGGLAVSISAGALSAAIADIMA ALKGPFKFGLWGVALYGVLPSQIAKDDPNMMSKIVTSLPA DDITESPVSSLPLDKATVNVNVRVVDDVKDERQNISVVSG VPMSCPVVDAKPTERPGVFTASIPGAPVLNISVNNSTPAV QTLSPGVTNNTDKDVRPAGFTQGGNTRDAVIRFPKDSGHN AVYVSVSDVLSPDQVKQRQDEENRRQQEWDATHPVEAAER NYERARAELNQANEDVARNQERQAKAVQVYNSRKSELDAA NKTLADAIAEIKQFNRFAHDPMAGGHRMWQMAGLKAQRAQ TDVNNKQAAFDAAAKEKSDADAALSSAMESRKKKEDKKRS AENNLNDEKNKPRKGFKDYGHDYHPAPKTENIKGLGDLKP GIPKTPKQNGGGKRKRWTGDKGRKIYEWDSQHGELEGYRA SDGQHLGSFDPKTGNQLKGPDPKRNIKKYL D:  GLKLDLTWFDKSTEDFKGEEYSKDFGDDGSVMESLGVPFK DNVNNGCFDVIAEWVPLLQPYFNHQIDISDNEYFVSFDYR DGDW Description Functional site 1) chain C residue 495 type sequence R description BINDING SITE FOR RESIDUE CIT C 601 source : AC1 2) chain C residue 519 type sequence Y description BINDING SITE FOR RESIDUE CIT C 601 source : AC1 3) chain C residue 544 type sequence K description BINDING SITE FOR RESIDUE CIT C 601 source : AC1 4) chain C residue 545 type sequence R description BINDING SITE FOR RESIDUE CIT C 601 source : AC1 5) chain C residue 546 type sequence N description BINDING SITE FOR RESIDUE CIT C 601 source : AC1 6) chain A residue 495 type sequence R description BINDING SITE FOR RESIDUE CIT A 602 source : AC2 7) chain A residue 519 type sequence Y description BINDING SITE FOR RESIDUE CIT A 602 source : AC2 8) chain A residue 545 type sequence R description BINDING SITE FOR RESIDUE CIT A 602 source : AC2 9) chain A residue 546 type sequence N description BINDING SITE FOR RESIDUE CIT A 602 source : AC2 10) chain A residue 550 type sequence Y description BINDING SITE FOR RESIDUE CIT A 602 source : AC2 11) chain A residue 510 type catalytic sequence D description 530 source MCSA : MCSA1 12) chain A residue 513 type catalytic sequence H description 530 source MCSA : MCSA1 13) chain A residue 517 type catalytic sequence E description 530 source MCSA : MCSA1 14) chain A residue 545 type catalytic sequence R description 530 source MCSA : MCSA1 15) chain C residue 510 type catalytic sequence D description 530 source MCSA : MCSA2 16) chain C residue 513 type catalytic sequence H description 530 source MCSA : MCSA2 17) chain C residue 517 type catalytic sequence E description 530 source MCSA : MCSA2 18) chain C residue 545 type catalytic sequence R description 530 source MCSA : MCSA2 19) chain A residue 513 type ACT_SITE sequence H description Proton donor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642 source Swiss-Prot : SWS_FT_FI1 20) chain C residue 513 type ACT_SITE sequence H description Proton donor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 517 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642 source Swiss-Prot : SWS_FT_FI2 22) chain C residue 517 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 545 type ACT_SITE sequence R description ACT_SITE => ECO:0000305|PubMed:11741540 source Swiss-Prot : SWS_FT_FI3 24) chain C residue 545 type ACT_SITE sequence R description ACT_SITE => ECO:0000305|PubMed:11741540 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 510 type SITE sequence D description Stabilizes positive charge on His-513 => ECO:0000305|PubMed:20852642 source Swiss-Prot : SWS_FT_FI4 26) chain C residue 510 type SITE sequence D description Stabilizes positive charge on His-513 => ECO:0000305|PubMed:20852642 source Swiss-Prot : SWS_FT_FI4

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