eF-site ID 3v5e-ABCDEFGHIJKLMN PDB Code 3v5e Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N click to enlarge Title Crystal structure of ClpP from Staphylococcus aureus in the active, extended conformation Classification HYDROLASE Compound ATP-dependent Clp protease proteolytic subunit Source null (CLPP_STAA8) Sequence A:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE B:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE C:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE D:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE E:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE F:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE G:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE H:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE I:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE J:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE K:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE L:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE M:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE N:  IPTVIERAYDIYSRLLKDRIIMLGSQIDDNVANSIVSQLL FLQAQDSEKDIYLYINSPGGSVTAGFAIYDTIQHIKPDVQ TICIGMAASMGSFLLAAGAKGKRFALPNAEVMIHQPLGGA QGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDT DRDNFLTAEEAKEYGLIDEVMVPE Description Functional site 1) chain B residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 2) chain C residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 3) chain D residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 4) chain E residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 5) chain F residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 6) chain G residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 7) chain H residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 8) chain I residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 9) chain J residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 10) chain K residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 11) chain L residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 12) chain M residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 13) chain N residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 98 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 16) chain C residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 17) chain D residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 18) chain E residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 19) chain F residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 20) chain G residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 21) chain H residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 22) chain I residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 23) chain J residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 24) chain K residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 25) chain L residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 26) chain M residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 27) chain N residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 123 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 90-101 type prosite sequence TICIGMAASMGS description CLP_PROTEASE_SER Endopeptidase Clp serine active site. TicIGmAASMGS source prosite : PS00381 30) chain A residue 112-125 type prosite sequence RFALPNAEVMIHQP description CLP_PROTEASE_HIS Endopeptidase Clp histidine active site. RfalPnaeVMIHQP source prosite : PS00382

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