eF-site ID 2hpo-A PDB Code 2hpo Chain A click to enlarge Title Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site Classification HYDROLASE Compound Aminopeptidase N Source Escherichia coli (strain K12) (AMPN_ECOLI) Sequence A:  PQAKYRHDYRAPDYQITDIDLTFDLDAQKTVVTAVSQAVR HGASDAPLRLNGEDLKLVSVHINDEPWTAWKEEEGALVIS NLPERFTLKIINEISPAANTALEGLYQSGDALCTQCEAEG FRHITYYLDRPDVLARFTTKIIADKIKYPFLLSNGNRVAQ GELENGRHWVQWQDPFPKPCYLFALVAGDFDVLRDTFTTR SGREVALELYVDRGNLDRAPWAMTSLKNSMKWDEERFGLE YDLDIYMIVAVDFFNMGAMENKGLNIFNSKYVLARTDTAT DKDYLDIERVIGHEYFHNWTGNRVTCRDWFQLSLKEGLTV FRDQEFSSDLGSRAVNRINNVRTMRGLQFAEDASPMAHPI RPDMVIEMNNFYTLTVYEKGAEVIRMIHTLLGEENFQKGM QLYFERHDGSAATCDDFVQAMEDASNVDLSHFRRWYSQSG TPIVTVKDDYNPETEQYTLTISQRTPATPDQAEKQPLHIP FAIELYDNEGKVIPLQKGGHPVNSVLNVTQAEQTFVFDNV YFQPVPALLCEFSAPVKLEYKWSDQQLTFLMRHARNDFSR WDAAQSLLATYIKLNVARHQQGQPLSLPVHVADAFRAVLL DEKIDPALAAEILTLPSVNEMAELFDIIDPIAIAEVREAL TRTLATELADELLAIYNANYQSEYRVEHEDIAKRTLRNAC LRFLAFGETHLADVLVSKQFHEANNMTDALAALSAAVAAQ LPCRDALMQEYDDKWHQNGLVMDKWFILQATSPAANVLET VRGLLQHRSFTMSNPNRIRSLIGAFAGSNPAAFHAEDGSG YLFLVEMLTDLNSRNPQVASRLIEPLIRLKRYDAKRQEKM RAALEQLKGLENLSGDLYEKITKALA Description Functional site 1) chain A residue 297 type sequence H description BINDING SITE FOR RESIDUE ZN A 1250 source : AC1 2) chain A residue 301 type sequence H description BINDING SITE FOR RESIDUE ZN A 1250 source : AC1 3) chain A residue 320 type sequence E description BINDING SITE FOR RESIDUE ZN A 1250 source : AC1 4) chain A residue 58 type sequence D description BINDING SITE FOR RESIDUE GOL A 1270 source : AC2 5) chain A residue 59 type sequence L description BINDING SITE FOR RESIDUE GOL A 1270 source : AC2 6) chain A residue 97 type sequence E description BINDING SITE FOR RESIDUE GOL A 1270 source : AC2 7) chain A residue 98 type sequence I description BINDING SITE FOR RESIDUE GOL A 1270 source : AC2 8) chain A residue 99 type sequence S description BINDING SITE FOR RESIDUE GOL A 1270 source : AC2 9) chain A residue 532 type sequence L description BINDING SITE FOR RESIDUE GOL A 1271 source : AC3 10) chain A residue 546 type sequence W description BINDING SITE FOR RESIDUE GOL A 1271 source : AC3 11) chain A residue 563 type sequence S description BINDING SITE FOR RESIDUE GOL A 1271 source : AC3 12) chain A residue 566 type sequence D description BINDING SITE FOR RESIDUE GOL A 1271 source : AC3 13) chain A residue 567 type sequence A description BINDING SITE FOR RESIDUE GOL A 1271 source : AC3 14) chain A residue 570 type sequence S description BINDING SITE FOR RESIDUE GOL A 1271 source : AC3 15) chain A residue 121 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 16) chain A residue 261 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 17) chain A residue 297 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 18) chain A residue 301 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 19) chain A residue 320 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 20) chain A residue 298 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:16885166, ECO:0000305|PubMed:18416562, ECO:0000305|PubMed:19622865 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 294-303 type prosite sequence VIGHEYFHNW description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIGHEYFHNW source prosite : PS00142 22) chain A residue 381 type SITE sequence Y description Transition state stabilizer => ECO:0000305 source Swiss-Prot : SWS_FT_FI3

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