eF-site ID 2cho-ABCD PDB Code 2cho Chain A, B, C, D click to enlarge Title Bacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activity Classification HYDROLASE Compound GLUCOSAMINIDASE Source Bacteroides thetaiotaomicron (2CHO) Sequence A:  LQPPPQQLIVQNKTIDLPAVYQLNGGEEANPHAVKVLKEL LGMLISIGEKGDKSVRKYSRQIPDHKEGYYLSVNEKEIVL AGNDERGTYYALQTFAQLLKDGKLPEVEIKDYPSVRYRGV VEGFYGTPWSHQARLSQLKFYGKNKMNTYIYGPKDDPYHS APNWRLPYPDKEAAQLQELVAVANENEVDFVWAIHPGQDI KWNKEDRDLLLAKFEKMYQLGVRSFAVFFDDISGEGTNPQ KQAELLNYIDEKFAQVKPDINQLVMCPTEYNKSWSNPNGN YLTTLGDKLNPSIQIMWTGDRVISDITRDGISWINERIKR PAYIWWNFPVSDYVRDHLLLGPVYGNDTTIAKEMSGFVTN PMEHAESSKIAIYSVASYAWNPAKYDTWQTWKDAIRTILP SAAEELECFAMHNSDLGPNGHGYRREESMDIQPAAERFLK AFKEGKNYDKADFETLQYTFERMKESADILLMNTENKPLI VEITPWVHQFKLTAEMGEEVLKMVEGRNESYFLRKYNHVK ALQQQMFYIDQTSNQNPYQPGVKTATRVIKPLIDRTFATV VKFFNQKFNAHLDATTDYMPHKMNLPLQVKANRVLISPVE IELDAIYPGENIQINFRLSAGLQKAPVKFVRFQFVLTIEK K B:  LQPPPQQLIVQNKTIDLPAVYQLNGGEEANPHAVKVLKEL LGMLISIGEKGDKSVRKYSRQIPDHKEGYYLSVNEKEIVL AGNDERGTYYALQTFAQLLKDGKLPEVEIKDYPSVRYRGV VEGFYGTPWSHQARLSQLKFYGKNKMNTYIYGPKDDPYHS APNWRLPYPDKEAAQLQELVAVANENEVDFVWAIHPGQDI KWNKEDRDLLLAKFEKMYQLGVRSFAVFFDDISGEGTNPQ KQAELLNYIDEKFAQVKPDINQLVMCPTEYNKSWSNPNGN YLTTLGDKLNPSIQIMWTGDRVISDITRDGISWINERIKR PAYIWWNFPVSDYVRDHLLLGPVYGNDTTIAKEMSGFVTN PMEHAESSKIAIYSVASYAWNPAKYDTWQTWKDAIRTILP SAAEELECFAMHNSDLGPNGHGYRREESMDIQPAAERFLK AFKEGKNYDKADFETLQYTFERMKESADILLMNTENKPLI VEITPWVHQFKLTAEMGEEVLKMVEGRNESYFLRKYNHVK ALQQQMFYIDQTSNQNPYQPGVKTATRVIKPLIDRTFATV VKFFNQKFNAHLDATTDYMPHKMNLPLQVKANRVLISPVE IELDAIYPGENIQINFRLSAGLQKAPVKFVRFFVLTIEK C:  XXXXXXXXXXXXX D:  XXXXXXXXXXXXX Description (1)  GLUCOSAMINIDASE (E.C.3.2.1.52) Functional site 1) chain A residue 32 type sequence E description BINDING SITE FOR RESIDUE CA A1717 source : AC1 2) chain A residue 61 type sequence E description BINDING SITE FOR RESIDUE CA A1717 source : AC1 3) chain A residue 64 type sequence D description BINDING SITE FOR RESIDUE CA A1717 source : AC1 4) chain A residue 242 type sequence D description BINDING SITE FOR RESIDUE ACT A1718 source : AC2 5) chain A residue 282 type sequence Y description BINDING SITE FOR RESIDUE ACT A1718 source : AC2 6) chain A residue 337 type sequence W description BINDING SITE FOR RESIDUE ACT A1718 source : AC2 7) chain A residue 339 type sequence N description BINDING SITE FOR RESIDUE ACT A1718 source : AC2 8) chain B residue 32 type sequence E description BINDING SITE FOR RESIDUE CA B1716 source : AC3 9) chain B residue 61 type sequence E description BINDING SITE FOR RESIDUE CA B1716 source : AC3 10) chain B residue 64 type sequence D description BINDING SITE FOR RESIDUE CA B1716 source : AC3 11) chain B residue 242 type sequence D description BINDING SITE FOR RESIDUE ACT B1718 source : AC4 12) chain B residue 243 type sequence D description BINDING SITE FOR RESIDUE ACT B1718 source : AC4 13) chain B residue 278 type sequence C description BINDING SITE FOR RESIDUE ACT B1718 source : AC4 14) chain B residue 282 type sequence Y description BINDING SITE FOR RESIDUE ACT B1718 source : AC4 15) chain B residue 337 type sequence W description BINDING SITE FOR RESIDUE ACT B1718 source : AC4 16) chain B residue 339 type sequence N description BINDING SITE FOR RESIDUE ACT B1718 source : AC4 17) chain A residue 135 type sequence G description BINDING SITE FOR RESIDUE GOL A1719 source : AC5 18) chain A residue 136 type sequence F description BINDING SITE FOR RESIDUE GOL A1719 source : AC5 19) chain A residue 314 type sequence V description BINDING SITE FOR RESIDUE GOL A1719 source : AC5 20) chain A residue 339 type sequence N description BINDING SITE FOR RESIDUE GOL A1719 source : AC5 21) chain A residue 342 type sequence V description BINDING SITE FOR RESIDUE GOL A1719 source : AC5 22) chain A residue 344 type sequence D description BINDING SITE FOR RESIDUE GOL A1719 source : AC5 23) chain A residue 372 type sequence N description BINDING SITE FOR RESIDUE GOL A1719 source : AC5 24) chain A residue 137 type sequence Y description BINDING SITE FOR RESIDUE GOL A1720 source : AC6 25) chain A residue 344 type sequence D description BINDING SITE FOR RESIDUE GOL A1720 source : AC6 26) chain A residue 345 type sequence Y description BINDING SITE FOR RESIDUE GOL A1720 source : AC6 27) chain A residue 347 type sequence R description BINDING SITE FOR RESIDUE GOL A1720 source : AC6 28) chain A residue 550 type sequence Y description BINDING SITE FOR RESIDUE GOL A1720 source : AC6 29) chain A residue 551 type sequence Q description BINDING SITE FOR RESIDUE GOL A1720 source : AC6 30) chain B residue 137 type sequence Y description BINDING SITE FOR RESIDUE GOL B1717 source : AC7 31) chain B residue 344 type sequence D description BINDING SITE FOR RESIDUE GOL B1717 source : AC7 32) chain B residue 345 type sequence Y description BINDING SITE FOR RESIDUE GOL B1717 source : AC7 33) chain B residue 347 type sequence R description BINDING SITE FOR RESIDUE GOL B1717 source : AC7 34) chain B residue 550 type sequence Y description BINDING SITE FOR RESIDUE GOL B1717 source : AC7 35) chain B residue 551 type sequence Q description BINDING SITE FOR RESIDUE GOL B1717 source : AC7 36) chain B residue 136 type sequence F description BINDING SITE FOR RESIDUE GOL B1719 source : AC8 37) chain B residue 314 type sequence V description BINDING SITE FOR RESIDUE GOL B1719 source : AC8 38) chain B residue 339 type sequence N description BINDING SITE FOR RESIDUE GOL B1719 source : AC8 39) chain B residue 342 type sequence V description BINDING SITE FOR RESIDUE GOL B1719 source : AC8 40) chain B residue 344 type sequence D description BINDING SITE FOR RESIDUE GOL B1719 source : AC8 41) chain B residue 372 type sequence N description BINDING SITE FOR RESIDUE GOL B1719 source : AC8 42) chain A residue 135 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 242 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 282 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 337 type BINDING sequence W description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 344 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 372 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 166 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 242 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 282 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 337 type BINDING sequence W description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 344 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 372 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 54) chain B residue 135 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 55) chain B residue 166 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 243 type ACT_SITE sequence D description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01353, ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI1 57) chain B residue 243 type ACT_SITE sequence D description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01353, ECO:0000269|PubMed:16565725 source Swiss-Prot : SWS_FT_FI1

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