eF-site ID 3cjc-ADG PDB Code 3cjc Chain A, D, G click to enlarge Title Actin dimer cross-linked by V. cholerae MARTX toxin and complexed with DNase I and Gelsolin-segment 1 Classification Structural protein/Hydrolase Compound Actin, alpha skeletal muscle Source ORGANISM_COMMON: rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus; Sequence A:  DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRH QGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWD DMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVT HNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSF VTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYN SIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITAL APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ EYDEAGPSIVHR D:  LKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEV RDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERY LFLFRPNKVSVLDTYQYDDGCCGNDSFSREPAVVKFSSHS TKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLND VMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADT TATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYGLS NEMALAISDHYPVEVTLT G:  MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFT GDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIF TVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG VASGF Description (1)  Actin, alpha skeletal muscle, Deoxyribonuclease-1 (E.C.3.1.21.1), Gelsolin Functional site 1) chain D residue 39 type catalytic sequence E description 41 source MCSA : MCSA1 2) chain D residue 76 type catalytic sequence Y description 41 source MCSA : MCSA1 3) chain D residue 78 type catalytic sequence E description 41 source MCSA : MCSA1 4) chain D residue 134 type catalytic sequence H description 41 source MCSA : MCSA1 5) chain D residue 168 type catalytic sequence D description 41 source MCSA : MCSA1 6) chain D residue 212 type catalytic sequence D description 41 source MCSA : MCSA1 7) chain D residue 252 type catalytic sequence H description 41 source MCSA : MCSA1 8) chain D residue 18 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1748997, ECO:0000269|PubMed:3560229 source Swiss-Prot : SWS_FT_FI5 9) chain A residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 10) chain A residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 11) chain A residue 53-63 type prosite sequence YVGDEAQSKRG description ACTINS_1 Actins signature 1. YVGDEAQs.KRG source prosite : PS00406 12) chain A residue 356-364 type prosite sequence WITKQEYDE description ACTINS_2 Actins signature 2. WITKqEYDE source prosite : PS00432 13) chain A residue 104-116 type prosite sequence LLTEAPLNPKANR description ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR source prosite : PS01132 14) chain D residue 167-174 type prosite sequence GDFNADCS description DNASE_I_2 Deoxyribonuclease I signature 2. GDFNAdCS source prosite : PS00918 15) chain D residue 130-150 type prosite sequence IVALHSAPSDAVAEINSLYDV description DNASE_I_1 Deoxyribonuclease I signature 1. IVALHSAPsdavaEINsLyDV source prosite : PS00919 16) chain G residue 41 type BINDING sequence G description BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK source Swiss-Prot : SWS_FT_FI1 17) chain G residue 42 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK source Swiss-Prot : SWS_FT_FI1 18) chain G residue 73 type BINDING sequence E description BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK source Swiss-Prot : SWS_FT_FI1 19) chain G residue 85 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK source Swiss-Prot : SWS_FT_FI1 20) chain G residue 90 type BINDING sequence G description BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK source Swiss-Prot : SWS_FT_FI1 21) chain G residue 92 type BINDING sequence A description BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK source Swiss-Prot : SWS_FT_FI1 22) chain G residue 121 type BINDING sequence V description BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK source Swiss-Prot : SWS_FT_FI1 23) chain G residue 111 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 24) chain G residue 35 type MOD_RES sequence Y description Phosphotyrosine; by SRC; in vitro => ECO:0000269|PubMed:10210201 source Swiss-Prot : SWS_FT_FI3 25) chain D residue 67 type MOD_RES sequence V description Phosphotyrosine; by SRC; in vitro => ECO:0000269|PubMed:10210201 source Swiss-Prot : SWS_FT_FI3 26) chain D residue 65 type SITE sequence Y description Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme source Swiss-Prot : SWS_FT_FI4

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