eF-site ID 3lb9-ABC PDB Code 3lb9 Chain A, B, C click to enlarge Title Crystal structure of the B. circulans cpA123 circular permutant Classification HYDROLASE Compound Endo-1,4-beta-xylanase Source (XYNA_BACCI) Sequence A:  ATFTQYWSVRQSKRPTGSNATITFTNHVNAWKSHGMNLGS NWAYQVMATEGYQSSGSSNVTVWGASTDYWQNWTDGGGIV NAVNGSGGNYSVNWSNTGNFVVGKGWTTGSPFRTINYNAG VWAPNGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTYKG TVKSDGGTYDIYTTTRYNAPSI B:  ATFTQYWSVRQSKRPTGSNATITFTNHVNAWKSHGMNLGS NWAYQVMATEGYQSSGSSNVTVWGASTDYWQNWTDGGGIV NAVNGSGGNYSVNWSNTGNFVVGKGWTTGSPFRTINYNAG VWAPNGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTYKG TVKSDGGTYDIYTTTRYNAPSI C:  ATFTQYWSVRQSKRPTGSNATITFTNHVNAWKSHGMNLGS NWAYQVMATEGYQSSGSSNVTVWGASTDYWQNWTDGGGIV NAVNGSGGNYSVNWSNTGNFVVGKGWTTGSPFRTINYNAG VWAPNGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTYKG TVKSDGGTYDIYTTTRYNAPSI Description Functional site 1) chain A residue 51 type catalytic sequence E description 432 source MCSA : MCSA1 2) chain A residue 100 type catalytic sequence N description 432 source MCSA : MCSA1 3) chain A residue 134 type catalytic sequence Y description 432 source MCSA : MCSA1 4) chain A residue 143 type catalytic sequence E description 432 source MCSA : MCSA1 5) chain A residue 145 type catalytic sequence Y description 432 source MCSA : MCSA1 6) chain B residue 51 type catalytic sequence E description 432 source MCSA : MCSA2 7) chain B residue 100 type catalytic sequence N description 432 source MCSA : MCSA2 8) chain B residue 134 type catalytic sequence Y description 432 source MCSA : MCSA2 9) chain B residue 143 type catalytic sequence E description 432 source MCSA : MCSA2 10) chain B residue 145 type catalytic sequence Y description 432 source MCSA : MCSA2 11) chain C residue 51 type catalytic sequence E description 432 source MCSA : MCSA3 12) chain C residue 100 type catalytic sequence N description 432 source MCSA : MCSA3 13) chain C residue 134 type catalytic sequence Y description 432 source MCSA : MCSA3 14) chain C residue 143 type catalytic sequence E description 432 source MCSA : MCSA3 15) chain C residue 145 type catalytic sequence Y description 432 source MCSA : MCSA3 16) chain A residue 143 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:8019418 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 143 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:8019418 source Swiss-Prot : SWS_FT_FI1 18) chain C residue 143 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:8019418 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 51 type ACT_SITE sequence E description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063, ECO:0000269|PubMed:8019418 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 51 type ACT_SITE sequence E description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063, ECO:0000269|PubMed:8019418 source Swiss-Prot : SWS_FT_FI2 21) chain C residue 51 type ACT_SITE sequence E description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063, ECO:0000269|PubMed:8019418 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 140-150 type prosite sequence PLIEYYVVDSW description GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW source prosite : PS00776 23) chain A residue 48-59 type prosite sequence MATEGYQSSGSS description GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS source prosite : PS00777

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