eF-site ID 1azw-AB PDB Code 1azw Chain A, B click to enlarge Title PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI Classification AMINOPEPTIDASE Compound PROLINE IMINOPEPTIDASE Source Xanthomonas campestris pv. citri (Xanthomonas citri) (PIP_XANCI) Sequence A:  MRTLYPEITPYQQGSLKVDDRHTLYFEQCGNPHGKPVVML HGGPGGGCNDKMRRFHDPAKYRIVLFDQRGSGRSTPHADL VDNTTWDLVADIERLRTHLGVDRWQVFGGSWGSTLALAYA QTHPQQVTELVLRGIFLLRRFELEWFYQEGASRLFPDAWE HYLNAIPPVERADLMSAFHRRLTSDDEATRLAAAKAWSVW EGATSFLHVDEDFVTGHEDAHFALAFARIENHYFVNGGFF EVEDQLLRDAHRIADIPGVIVHGRYDVVCPLQSAWDLHKA WPKAQLQISPASGHSAFEPENVDALVRATDGFA B:  MRTLYPEITPYQQGSLKVDDRHTLYFEQCGNPHGKPVVML HGGPGGGCNDKMRRFHDPAKYRIVLFDQRGSGRSTPHADL VDNTTWDLVADIERLRTHLGVDRWQVFGGSWGSTLALAYA QTHPQQVTELVLRGIFLLRRFELEWFYQEGASRLFPDAWE HYLNAIPPVERADLMSAFHRRLTSDDEATRLAAAKAWSVW EGATSFLHVDEDFVTGHEDAHFALAFARIENHYFVNGGFF EVEDQLLRDAHRIADIPGVIVHGRYDVVCPLQSAWDLHKA WPKAQLQISPASGHSAFEPENVDALVRATDGFA Description Functional site 1) chain A residue 100 type sequence G description ACTIVE-SITE. source : AS 2) chain A residue 266 type sequence D description ACTIVE-SITE. source : AS 3) chain A residue 294 type sequence H description ACTIVE-SITE. source : AS 4) chain A residue 43 type catalytic sequence G description 412 source MCSA : MCSA1 5) chain A residue 110 type catalytic sequence S description 412 source MCSA : MCSA1 6) chain A residue 111 type catalytic sequence W description 412 source MCSA : MCSA1 7) chain A residue 266 type catalytic sequence D description 412 source MCSA : MCSA1 8) chain A residue 294 type catalytic sequence H description 412 source MCSA : MCSA1 9) chain B residue 43 type catalytic sequence G description 412 source MCSA : MCSA2 10) chain B residue 110 type catalytic sequence S description 412 source MCSA : MCSA2 11) chain B residue 111 type catalytic sequence W description 412 source MCSA : MCSA2 12) chain B residue 266 type catalytic sequence D description 412 source MCSA : MCSA2 13) chain B residue 294 type catalytic sequence H description 412 source MCSA : MCSA2 14) chain A residue 110 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:9427736 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 110 type ACT_SITE sequence S description Nucleophile => ECO:0000269|PubMed:9427736 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 266 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:9427736 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 266 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:9427736 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 294 type ACT_SITE sequence H description Proton donor => ECO:0000269|PubMed:9427736 source Swiss-Prot : SWS_FT_FI3 19) chain B residue 294 type ACT_SITE sequence H description Proton donor => ECO:0000269|PubMed:9427736 source Swiss-Prot : SWS_FT_FI3

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